Synthetic long peptides (slp) for therapeutic vaccination against hepatitis b virus infection

ABSTRACT

The present invention relates to the fields of medicine and immunology. In particular, it relates to novel peptides that may be used in the treatment and/or prevention of a Hepatitis B viral infection and/or an Hepatitis B related disease or condition.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a divisional of U.S. patent application Ser. No. 15/315,526, filed Dec. 1, 2016, published Aug. 31, 2017 as US 2017/0246293 A1, which is a National Phase of International Patent Application No. PCT/NL2015/050390, filed Jun. 1, 2015, published on Dec. 10, 2015 as WO 2015/187009 A1, which claims priority to European Patent Application No. 14170733.1, filed Jun. 2, 2014. The contents of these applications are herein incorporated by reference in their entirety.

SEQUENCE LISTING

The instant application contains a Sequence Listing which has been submitted in ASCII format via EFS-WEB and is hereby incorporated by reference in its entirety. Said ASCII copy, created on May 8, 2017, is named 069818_2180SequenceListing.txt and is 412 KB.

FIELD OF THE INVENTION

The present invention relates to the fields of medicine and immunology. In particular, it relates to novel peptides that may be used in the treatment and/or prevention of a Hepatitis B viral infection and/or an Hepatitis B related disease or condition.

BACKGROUND OF THE INVENTION

Chronic infection with the hepatitis B virus (HBV) is a major global health problem. HBV is the prototype member of the Hepadnaviridae family, which have a strong preference for infecting liver cells (Ganem et al, 2004).

Despite the availability since three decades of an efficacious preventive vaccine for the protection against hepatitis B, an estimated two billion people have nevertheless been infected with HBV and more than 240 million currently have chronic (long-term) hepatitis B infection, with a geographical predominance in regions outside Western Europe and North America (World Health Organization, July 2013).

Transmission of the virus between people occurs by direct blood-to-blood contact or via semen or vaginal fluid of an infected person. In endemic areas, the infection occurs characteristically by perinatal transmission from mother to child. Thus, although HBV is not transmitted casually, the virus—via similar modes of entry as human immunodeficiency virus (HIV) but being at least 50 times more infectious—can be easily transmitted by perinatal, percutaneous or sexual exposure. Frequent person-to-person contact with infected individuals accordingly poses a serious risk to groups like health workers.

Infection with HBV can develop as an acute viral hepatitis, an illness that begins with general ill-health, loss of appetite, nausea, vomiting, body aches, mild fever, and dark urine, and then progresses to development of jaundice. The illness lasts for a few weeks and then gradually improves in most affected adults. A few people may have more severe liver disease (fulminant hepatic failure), and may die as a result. The infection may be entirely asymptomatic and may go unrecognized. Chronic infection with hepatitis B virus either may be asymptomatic or may be associated with a chronic inflammation of the liver (chronic hepatitis), leading to cirrhosis over a period of many years. This type of infection dramatically increases the incidence of hepatocellular carcinoma (liver cancer), also with a latency of many years.

Treatment of chronically HBV-infected individuals with antiviral drugs such as nucleoside/nucleotide analogues (e.g. Entecavir and Tenofovir) or interferon (IFN)α efficiently decreases serum viral loads. However, antiviral therapy rarely leads to a sustained virological response and drug resistance occurs (Zoulim et al., 2012). Moreover, the great majority of HBV carriers remains untreated.

Approximately 15-40% of chronic HBV carriers will develop clinically significant liver diseases in their lifetime with a high risk of death from liver cirrhosis and associated liver failure or hepatocellular carcinoma (HCC) (Lok, 2002; and Huang et al., 2011). Yearly up to one million people die worldwide due to the acute or chronic consequences of hepatitis B (Michel et al, 2001; Grimm et al, 2013). Due to the failure of antiviral drugs to eradicate infection, and consequently the need for long-term if not lifelong antiviral therapy with its drawbacks such as toxic side-effects and high costs, there is an urgent need for novel therapeutic approaches (Grimm et al., 2013).

The present invention is meant to enable efficacious therapeutic vaccination against chronic HBV infection. Therapeutic vaccination constitutes a promising strategy to treat chronic hepatitis B (Michel et al., 2011).

Next to the humoral immune response against HBV, which is predominantly involved in the protection against HBV infection by the current prophylactic vaccines (Lok, 2002), the cellular immune response is unequivocally involved in the natural resistance against HBV infection.

Perinatal transmission of HBV from mothers to neonates and infections during the first years of life result in persistent infection in more than 90% of children. By contrast, infection during adulthood clears spontaneously in more than 90% of cases and results in lifelong protective immunity (Rehermann et al., 2005).

In acute, self-limited hepatitis B virus infection, vigorous polyclonal and multispecific CD8⁺ cytotoxic T cell (CTL) and CD4⁺ T-helper (Th) cell responses to many HBV antigens are readily demonstrable in the peripheral blood (Michel et al., 2011).

These T cell responses are crucial in HBV clearance and control. Experiments in HBV-infected chimpanzees have shown the essential role of HBV-specific CD8⁺ T cells as effector cells in this process (Thimme et al., 2003). In contrast to the response in patients with resolved HBV infections, in patients with chronic hepatitis B the T cell responses are usually very weak, focused on only a few epitopes and functionally impaired (Michel et al., 2011). The goal of therapeutic vaccination is to install vigorous and robust multivalent CTL and T-helper cell responses directed to many HBV antigens, thereby pursuing viral clearance, hepatitis control and cure.

Despite the fact that great progress has been made in understanding the etiology and epidemiology of the disease, there is still a need for an effective therapeutic HBV vaccine.

DETAILED DESCRIPTION OF THE INVENTION

The inventors identified a selection of HBV antigens to be used for efficacious therapeutic vaccination. Based on HLA class I and class II binding capacities of HBV protein-derived peptides and analysis of the generation of these HLA class I binding peptides by cleavages made by the proteasome, the most immunogenic regions, covering a very high percentage of all possible T cell epitopes in the global hepatitis B patient population, have been uncovered in the HBV polymerase protein, core protein, X protein and large surface protein. These regions contain high numbers of T cell epitopes and when administered to the hepatitis B patient—either as chemically synthesized long peptide or via genetic approaches—such a vaccination is envisioned to induce a vigorous T cell response, resolving the HBV infection.

The use of relatively short peptides is highly preferred for medical purposes as these can be efficiently synthesized in vitro, which is not possible or uneconomical for native proteins larger than approximately 100, i.e. 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105 amino acids. Chemical synthesis of peptides is routine practice and various suitable methods are known to the skilled person. Chemical synthesis of peptides also overcomes the problems associated with recombinant production of intact proteins, which is difficult to standardize and requires extensive purification and quality control measures. Peptides with a length that exceeds the length of human leukocyte antigen (HLA) class I and class II epitopes (e.g. having a length as indicated below herein) are particularly advantageous for use as vaccine component because they are large enough to be taken up by professional antigen presenting cells (APC), in particular Dendritic cell (DC), as explained in WO02/070006, and processed in the DC before cell surface presentation of the contained HLA class I-presented and HLA class II-presented epitopes takes place. Therefore, the disadvantageous induction of T cell tolerance by the systemic presentation of minimal HLA class I-presented epitopes on non-antigen presenting cells (as shown in Toes et al., 1996a, and Toes et al., 1996b), is prevented by the application of peptides exceeding the length of human leukocyte antigen (HLA) class I and class II epitopes (as shown in Zwaveling et al., 2002).

The present invention relates to novel peptides of about 15 to about 100 amino acids in length, also denominated herein as long peptides, that each exceed the length of human leukocyte antigen (HLA) class I and class II presented epitopes and that induce a combined CD4⁺ and CD8⁺ T cell response that is therapeutically successful and inducing cure in a high percentage of patients. Preferably, the long peptides of the invention are synthetic peptides, denominated herein as synthetic long peptides (SLPs). As compared to vaccination with the peptides of the present invention, therapeutic vaccination with full length HBV proteins is likely to be less potent (Rosalia et al., 2013). From the viewpoint of manufacture and administration of peptides to patients, immunization with the complete set of overlapping long peptides or SLPs spanning the full length HBV polymerase, HBV core protein, HBV X protein and HBV large surface protein is not feasible. To narrow the number of peptides in a vaccine, it is needed to incorporate the most immunogenic SLPs that are recognized by the highest percentage of patients. The present invention provides for peptides and peptide vaccines to meet this need. Using a stepwise sophisticated selection procedure based on bioinformatics analyses that are experimentally underpinned, the long peptide and/or SLP sequences with the highest coverage of HLA class I-restricted cytotoxic T lymphocyte epitopes and HLA class II-restricted T helper epitopes were identified. The selections as described herein identify the long peptide and/or SLP sequences that incorporate HBV-derived T cell epitopes that are presented on all predominantly expressed HLA class I and class II alleles. By covering the vast majority of worldwide expressed HLA haplotypes (Bui et al., 2006), the long peptide and/or SLP vaccine composition can be used in all HBV infected individuals. The present invention describes the identification and selection of HBV-derived long peptides, preferably SLPs, that are highly immunogenic and capable of inducing a potent combined HBV-directed CD4⁺ T helper and CD8⁺ cytotoxic T cell response, when administered as a vaccine composition to patients. Such highly immunogenic long peptides from HBV have not been disclosed in the prior art. The HBV-derived long peptides of the invention were identified based on a putative immunogenicity score developed and validated by the inventors and as disclosed herein. The putative immunogenicity is quantified herein using the T cell Regional Immunogenicity Assessment (TRIA) score. The TRIA score is based on the cumulative Class I-BCI score of said peptide, which is indicative for their immunogenic CTL activating capacity, and the cumulative Class II-B score of said peptide, which is indicative for their immunogenic Th-cell activating capacity. Calculation of the cumulative Class I-BCI score and the cumulative Class II-B score is described in detail herein in the Examples section. The TRIA score is calculated as the sum of the cumulative Class I-BCI score and the cumulative Class II-B score. A strong correlation was found between this TRIA score and the T cell responses found in PBMC of HBV-immune donors. Therefore, the TRIA score enables the selection of optimal immunogenic long peptides.

In a first aspect, the present invention provides a peptide derived from an HBV protein. Preferably the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-79, 1142-1145 and 1468-1471, more preferably the peptide of the invention comprises or consist of a peptide selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 76, 77, 1142 and 1469, more preferably selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 77, 1142 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 76, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 60, 63, 71, 74, 75 and 1469, most preferably selected from the group of SEQ ID NO: 75, 1469 and 63. Further preferred is a peptide of the invention that comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51, 60, 63, 64, 68, 71, 74-77. Also preferred is a peptide of the invention that comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 63, 71 and 75. Preferably, the peptide of the invention comprises at least about 70 predicted T-cell epitopes. More preferably, the peptide of the invention comprises at least about 70 predicted T-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, the peptide if the invention comprises at least about 70 predicted HLA class I-restricted CD8⁺ cytotoxic T-cell epitopes, at least about 1 predicted HLA class II-restricted CD4⁺ T-helper epitope. More preferably, the peptide if the invention comprises at least about 70 predicted HLA class I-restricted CD8⁺ cytotoxic T-cell epitopes, at least about 1 predicted HLA class II-restricted CD4⁺ T-helper epitope and at least about 3 proteasomal cleavage sites. HLA class I-restricted CD8⁺ cytotoxic T-cell epitope is also denominated herein as CTL epitope and HLA class II-restricted CD4⁺ T-helper epitope is also denominated herein as Th-cell epitope. Preferably, the peptide of the invention comprises at least about 70 predicted CTL epitopes, at least about 15 predicted Th-cell epitopes. More preferably, the peptide of the invention comprises at least about 70 predicted CTL epitopes, at least about 15 predicted Th-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises at least about 95 predicted CTL epitopes, at least about 25 predicted Th-cell epitopes. More preferably, the peptide of the invention comprises at least about 95 predicted CTL epitopes, at least about 25 predicted Th-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises at least about 125 predicted CTL epitopes, at least about 50 predicted Th-cell epitopes. More preferably, a peptide of the invention comprises at least about 125 predicted CTL epitopes, at least about 50 predicted Th-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, a peptide of the invention has a TRIA score of at least about 6300, at least about 8000, at least about 9000, at least about 10000, or preferably at least about 14000.

A peptide of the invention can advantageously be used in the prevention and/or treatment of an HBV related disease or condition in a subject, preferably a mammal, more preferably a human. Preferably, the peptide of the invention comprises or consists of an amino acid sequence, preferably a contiguous amino acid sequence, of any of the proteins selected from the group consisting of HBV protein polymerase, HBV core protein, HBV X-protein and HBV large surface protein. Preferably, said peptide comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-79, 1142-1145 and 1468-1471. A peptide of this group is characterized in that it has a TRIA score of at least 6300, indicating the high immunogenic capacity for CD4+ and CD8+ T cell activation. Furthermore, a peptide of this group is characterized in that it comprises at least 70 predicted HLA class I-restricted CD8⁺ cytotoxic T-cell epitopes, at least 1 predicted HLA class II-restricted CD4⁺ T-helper epitope. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites.

More preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-53, 55-57, 60-66, 68-78, 1142-1145 and 1468-1471. A peptide of this group is characterized in that it has a TRIA score of at least 8000.

More preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-53, 55-57, 60-66, 68, 69, 71-79, 1142-1145 and 1468-1471. A peptide of this group is characterized in that it comprises at least 70 predicted CTL epitopes, at least 15 predicted Th-cell epitopes. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-53, 55, 57, 60, 63, 64, 66, 68, 71, 72, 74-78, 1142, 1145, 1468-1471.

More preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 53, 55-57, 60-66, 68, 69, 71, 73-78, 1142-1145, 1468-1471. A peptide of this group is characterized in that it has a TRIA score of at least 9000.

Even more preferably, the peptide of the invention is a peptide that comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 55-57, 60-65, 68, 69, 71, 74, 75, 77, 78, 1142-1145, 1468, 1469 and 1471. A peptide of this group is characterized in that it has a TRIA score of at least 10000.

Even more preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 52, 53, 55, 57, 60, 61, 63, 64, 68, 69, 71, 72, 75, 77, 78, 1142-1145, 1468, 1469 and 1471. A peptide of this group is characterized in that it comprises at least 95 predicted CTL epitopes, at least 25 predicted Th-cell epitopes. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 75, 77, 1142, 1469.

Most preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 63, 75, 1143-1145, 1468 and 1469. A peptide of this group is characterized in that it has a TRIA score of at least 14000. Furthermore, a peptide of this group is characterized in that it comprises at least 125 predicted CTL epitopes, at least 50 predicted Th-cell epitopes. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites.

A “T-cell epitope” is defined herein as a linear fragment of a polypeptide antigen, which is recognized and bound by a T-cell receptor, preferably a human T-cell receptor, after being made accessible to a T-cell receptor by intracellular proteolytic processing of the polypeptide antigen and subsequent presentation by an HLA class I or HLA class II molecule on the cell surface of an antigen-presenting cell. A “predicted T-cell epitope” is to be understood herein as a linear fragment of a polypeptide antigen for which liberation from the source protein or peptide by proteolytic cleavage and T-cell receptor recognition and/or binding has been predicted using bioinformatics analyses based on algorithms that predict HLA class I and II peptide binding and C-terminal generation by the proteasome of all possible HLA class I binding peptides (with a length of a HLA class I ligand; 8-12 aa) contained in the HBV proteins. A “confirmed T-cell epitope” is to be understood herein as a linear fragment of a polypeptide antigen for which liberation from the source protein or source polypeptide by proteolytic cleavage and T-cell receptor recognition and/or binding, and more preferably CD4⁺ or CD8⁺ T cell activation capability, have been established experimentally as disclosed herein. A “linear fragment” is understood herein to be a contiguous amino acid sequence of a polypeptide antigen, said polypeptide antigen preferably being an HBV protein, more preferably a protein selected from the group consisting of HBV protein polymerase, HBV core protein, HBV X-protein and HBV large surface protein. An identical linear fragment of a polypeptide antigen showing binding affinity to a second or further type of HLA class I or HLA class II molecule is to be understood herein as a second or further T-cell epitope. In other words, a specific linear fragment of a polypeptide antigen being capable to bind to two types of HLA molecules is understood herein to be two separate or distinct T-cell epitopes, and is scored twice within the cumulative BCI Class I- and/or Class II-B score. A T-cell epitope typically comprises or consists of at least 8 amino acids and up to 20 or (exceptionally) even more amino acids. A T-cell epitope can be an HLA class I-restricted CD8⁺ cytotoxic T cell (CTL) epitope or an HLA class II-restricted CD4⁺ T-helper (Th−)cell epitope. HLA class I restricted epitopes (also referred to as CTL epitopes) are typically presented via the classical proteasome dependent HLA class I processing route, whereas HLA class-II molecules are typically loaded with linear fragments in the late endosomal compartment. Preferably, a peptide according to the invention comprises T-cell epitopes that are selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466 (see Tables 4-7). A preferred peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. A more preferred peptide according to the invention comprises at least 95, 96, 97, 98, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. An even more preferred peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466. An even more preferred peptide according to the invention comprises at least 95, 96, 97, 98, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466. Preferably, the predicted T-cell epitopes of the present invention are confirmed experimentally as disclosed herein. A preferred peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 confirmed T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. A more preferred peptide according to the invention comprises at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. An even more preferred peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 confirmed T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466. An even more preferred peptide according to the invention comprises at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466.

A “proteasomal cleavage site” is understood herein as a site in a protein or polypeptide that is cleaved by the proteasome, preferably a human proteasome/proteasome naturally present in a human cell. A specific proteasomal cleavage site liberating the C-terminus of the epitope is preferably present exactly after the C-terminus of the epitope amino acid sequence, in order to allow the epitope's C-terminal residue to be liberated from the larger peptide and to be presented by the HLA class I molecule. The first important event that defines an HLA class I-restricted CD8⁺ cytotoxic T-cell (CTL) epitope is the release of the epitope (or the epitope-precursor) from its flanking protein regions through enzymatic cleavage by cytosolic peptidases. The multicatalytic proteasome is the primary enzyme complex required for the generation of the exact C-terminus of the vast majority of CTL epitopes (Rock et al., 2004). Proteasomes are multicatalytic enzyme complexes abundantly present intracellularly and are considered responsible for the generation of the C terminus of the vast majority of CTL epitopes (Craiu et al, 1997; Stoltze et al., 1998; Mo et al., 1999). The generation of the amino-terminus of a CTL epitope, on the other hand, is much more flexible because several amino-terminal exo-peptidases (like ERAP1, puromycin sensitive aminopeptidase, bleomycin hydrolase and others) reside in the cytosol and endoplasmic reticulum and these trimming enzymes have the capacity to shorten an N-terminal elongated epitope-precursor to its precise length. In contrast, C-terminal trimming has not been reported. Therefore the identification of the proteasome-mediated cleavage sites in a protein or in a polypeptide, like a peptide of the invention, can be used as an important identifier of almost every CTL epitope, because the proteasomal cleavages determine and enable C-terminal epitope generation (Kessler et al., 2001; Kessler and Melief, 2007). The assessment of proteasomal cleavage sites in the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein identifies the C-termini of intracellularly produced HBV peptide fragments, specifically for HLA class I presented peptide fragments. Length requirements are much less strict for loading of HLA class II with peptide fragments. Therefore, precise enzymatic generation of the HLA class II binding peptide fragment is not needed. These T-cell epitope requirements have been used in the present invention to localize and design long peptides derived from the full length sequences of an HBV protein which comprises preferred CD8⁺ cytotoxic T cell (CTL) and CD4⁺ T-helper (Th−)cell epitopes and/or combinations thereof and are thus highly immunogenic and therefore suitable peptides for synthesis and (therapeutic) vaccination purposes.

Proteasome mediated proteolytic cleavages can be predicted in silico using a prediction algorithm. Cleavage as performed by the proteasome can be verified in a proteasome mediated cleavage assay as disclosed herein, which measures the C-terminal liberation of the epitope from its flanking regions (Kessler et al., 2001; Kessler and Melief, 2007). A cell free proteasome cleavage assay identifying and quantitatively measuring the amino acid (aa) positions and the abundancy of cleavages by the proteasome in a polypeptide can be used to determine which peptides are generated from the source protein (or source polypeptide), thereby establishing the peptide pool available for epitope generation. The cell free proteasome cleavage assay involves the co-incubation of a polypeptide (preferably having a length of 28-40 aa, more preferably having a length of 30-39 aa) with a preparation of purified proteasomes in an appropriate buffer solution. Two main forms of proteasomes exist, the immunoproteasomes, which are mainly expressed in professional antigen presenting cells, like e.g. Dendritic Cells, and the constitutive proteasomes, which are expressed mainly in other cell types. These types contain variant catalytic subunits with slightly different catalytic activity. Although most epitopes are liberated by both types of proteasomes, sometimes differential epitope generation occurs dependent on proteasome type (Morel et al., 2000; Chapiro et al., 2006). Accordingly, proteasome-mediated cleavage assays may be performed separately with these two proteasome types. Preferably, a constitutive 20S-proteasome or immune 20S-proteasome is used as disclosed herein. The reaction mixture comprising the peptides to be cleaved and either of the two proteasome types (purified proteasome preparations) is incubated at 37° C. and samples are drawn at 1 h, 3 h, 6 h and 24 h time points as detailed in the Examples herein. Subsequently, generated peptide cleavage fragments and the remaining source polypeptide are identified and quantified by mass spectrometry (Kessler et al., 2001). This assay reveals both the positions in the polypeptide (and thus in the source protein) where the proteasome cleaves and the cleavage efficiency (abundancy) at these positions. A cleavage site can be confirmed by detection of fragments containing as COOH terminus the residue NH2-terminal from the cleavage site together with the (possible) complementary fragment(s), as calculated from the intensities of the fragment peaks in the mass spectra (preferably present for >1%, more preferably present for ≥7%, at 24 h incubation), in both the digestion with constitutive proteasomes and the digestion with immunoproteasomes. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more, preferably at least 3, proteasomal cleavage site as defined herein. More preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more, preferably at least 3, proteasomal cleavage site as assessed and verified in a proteasomal cleavage assay as described above.

As indicated above, examples of T-cell epitopes are HLA class I-restricted CD8⁺ cytotoxic T cell (CTL) epitopes and HLA class II-restricted CD4⁺ T-helper (Th−)cell epitopes. A “CTL epitope” is understood herein as a linear fragment of a polypeptide antigen that is liberated from the source protein by proteasome mediated proteolytic cleavage and subsequently presented by an HLA class I molecule on the cell surface of an antigen presenting cell (APC), preferably a human antigen presenting cell. A “predicted CTL epitope” is understood herein as a linear fragment of a polypeptide antigen for which liberation from its source protein by proteolytic cleavages and HLA class I molecule binding have been predicted using bioinformatics analyses based on algorithms that predict HLA class I peptide binding and C-terminal generation by the proteasome of all HLA class I binding short peptides (with a length of a CTL epitope; 8-12 aa) contained in the HBV proteins. Preferably, a predicted CTL epitope of the present invention is confirmed experimentally as disclosed herein. A CTL epitope of the invention is preferably capable of activating a CD8⁺ T cell response. A “confirmed CTL epitope” is understood herein as a linear fragment of a polypeptide antigen for which liberation by proteolytic cleavages and HLA class I molecule binding, more preferably CD8⁺ T cell activation, have been established experimentally as disclosed herein. A CTL epitope of the invention is preferably capable of activating a CD8⁺ T cell response. A CTL epitope typically comprises at least 8 up to 12, or exceptionally up to 13 or 14 amino acids. Preferably a CTL epitope consists of 8-14 amino acids, i.e. has a length of at least 8 up to 14 amino acids.

A CTL epitope is defined by two important intracellular events being (i) proteasome mediated proteolytic cleavage and (ii) binding to an HLA class I molecule, which takes place in the endoplasmic reticulum (ER). The stronger a linear peptide fragment binds and the slower the off-rate, the more likely that this linear peptide fragment will become a cell surface presented immunogenic CTL epitope (Van der Burg et al., 1996). Analysis of proteasome mediated proteolytic cleavages can be performed as indicated above. Preferably, specific binding to an HLA class I molecule is predicted using an in silico prediction algorithm and established by using an HLA class I peptide binding assay as known by the person skilled in the art (Kessler and Melief, 2007; Kessler et al., 2003). Preferably, the HLA class I-restricted epitope in a long peptide according to the invention is predicted to be generated at its C-terminus by the proteasome and preferably has a predicted high affinity binding capacity for the HLA class I molecule using an assay as described in van der Burg et al., 1995 and Kessler et al., 2003; e.g. IC₅₀≤about 5 μM may be considered high affinity binding, about 5 μM<IC₅₀≤about 15 μM may be considered intermediate affinity binding, about 15 μM<IC₅₀≤100 μM may be considered low affinity binding and IC₅₀>about 100 μM may be considered as no binding. To measure class I binding affinity of a peptide or fragments thereof, various HLA class I binding assays are available. The assays can be divided into cell-free assays (using soluble HLA) versus cellular assays (using HLA class I molecules on the cell surface), and competitive assays (resulting in semi-quantitative data) versus assays that do not use a labeled reference peptide and are therefore quantitative (Kessler and Melief, 2007; Viatte et al., 2006). The assays have in common that the HLA class I peptide binding affinity is reliably assessed.

The actual presentation of a CTL epitope on the cell surface, i.e. the net result of both proteasomal cleavage, possible other proteolytic events like N-terminal trimming, and binding and presentation by an HLA class I molecule, which events together define a CTL epitope as indicated above, can be demonstrated by a biochemical approach or by a functional approach using cytotoxic T cells with a T-cell receptor specific for the epitope and HLA class I molecule (geno)type, as known by the person skilled in the art (Kessler and Melief, 2007).

The biochemical approach involves the biochemical purification of HLA-epitope complexes from cells expressing the HBV antigen of the invention together with the presenting HLA class I molecule (geno)type, followed by the mass spectrometric search for the epitope in the eluted HLA class I-bound CTL receptor ligands as known by the person skilled in the art (Schirle et al., 2000; Schirle et al., 2001).

The functional approach involves a CTL line or clone that is specifically recognizing the HLA-epitope, which is used as a tool to demonstrate the natural processing and actual presentation of the epitope by HLA class I molecules. In this methodology, using a CTL induction assay as known in the art, either the synthetically generated minimal (i.e. exact length) epitope or the peptide sequence of interest encompassing the epitope, for instance a peptide, long peptides and/or SLP as defined herein, is used to stimulate and select HLA-epitope-specific cytotoxic T cells. To that end, briefly, a multivalent CD8⁺ T cell population, or a multivalent mixed CD8⁺ and CD4⁺ T cell population, is stimulated with autologous target cells of which the HLA class I molecules on the cell surface are either exogenously loaded with the precise synthetic epitope or endogenously loaded with intracellularly generated CTL epitopes derived from the exogenously loaded long peptide of the invention after its uptake by the antigen presenting target cells. In case the autologous target cells are loaded with a peptide, e.g. the synthetic long peptide of the invention, or fragments thereof, encompassing the epitope, the epitope is generated after cellular uptake of the peptide and its intracellular processing by the proteasome together with other N-terminal trimming peptidases. Subsequently, using a T cell recognition assay, the HLA-epitope-specific CTL is used to demonstrate the intracellular generation and natural presentation of the epitope of the invention by HLA class I molecules on the surface of HBV-infected cells. Specific recognition of an HLA class I restricted epitope by a CTL demonstrates the cell surface expression of the epitope and reveals its immunogenicity, i.e. the presence of epitope-specific T cells in the (T-cell receptor) repertoire of a selected donor. Preferably, the CD8⁺ T cell activating capability has been demonstrated ex vivo and/or in vivo, in T cells from human healthy control individuals or even more preferably in T cells from a human patient with an HBV related disease or condition and/or from a healthy control. The activation is preferably assessed ex vivo or in vivo, more preferably in a human patient with an HBV related disease. A CTL epitope for which liberation by proteolytic cleavage and HLA class I molecules presentation, or preferably CD8⁺ T cell activating capability, has been demonstrated experimentally is denominated herein as a confirmed CTL epitope.

A peptide of the invention preferably comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes as defined herein. Preferably, a peptide of the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes as defined herein. Preferably, a peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. More preferably a peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes from the HBV core protein, HBV polymerase, HBV X protein or HBV large surface protein. Even more preferably, a peptide according to the invention comprises or consists of a contiguous amino acid sequence of any of the proteins selected from the group consisting of HBV core protein, HBV polymerase, HBV X protein and HBV large surface protein, wherein said contiguous amino acid sequence comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes. Preferably, a peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 CTL predicted epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 (see Tables 4a, 5a, 6a and 7a). Even more preferably, a peptide of the invention preferably comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 40, 50, 60, 70, or preferably at least 95 confirmed CTL epitopes as defined herein and verified using a biochemical or functional assay as described above. Most preferred is a peptide of the invention that comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 or preferably at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed CTL epitopes as defined herein and verified using a functional assay as described above. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 or preferably at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395.

A “Th-cell epitope” is understood herein to be a linear peptide fragment that is recognized by an HLA class II molecule. A “predicted Th-cell epitope” is understood herein as a linear fragment of a polypeptide antigen for which HLA class II molecule recognition has been predicted using sophisticated bioinformatics analyses that are experimentally underpinned. Preferably, a predicted Th-cell epitope of the present invention is confirmed experimentally as disclosed herein. A Th-cell epitope of the invention is preferably capable of inducing a CD4⁺ T cell response. A “confirmed Th-cell epitope” is understood herein as a linear fragment of a polypeptide antigen for which HLA class II molecule recognition has been established experimentally as known by the person skilled in the art and further detailed herein.

An HLA class II-restricted CD4⁺ T-helper cell (Th-cell) epitope typically comprises 15 up to 20, or exceptionally even more, amino acids. Preferably, an HLA class II-restricted T-helper cell epitope comprises or 10-20 or 10-15 amino acids. Specific recognition of a predicted HBV-derived Th-cell epitope can be tested and/or verified in a Th-cell induction assay. To this end the peptide or fragment thereof, long peptide and/or SLP sequence of interest comprising the predicted Th-cell epitope is exogenously loaded on the surface of target cells and subsequently these peptide-loaded target cells are co-incubated with a multivalent autologous T helper cell population. After several rounds of stimulation, epitope-specific T helper cells can be selected and can be back-tested for the recognition of the T helper cell epitope contained in the peptide or SLP thereby proving its natural cell surface presentation. Preferably, an HLA class II-restricted CD4⁺ T-helper cell epitope comprised in a peptide according to the invention is capable of inducing or activating a CD4⁺ T-helper cell in a human patient with an HBV related disease or condition. The induction or activation is preferably assessed ex vivo or in vivo, more preferably in a human patient with an HBV related disease. Most preferably, the HLA class II-restricted epitope is capable of activating a CD4⁺ T-helper memory and/or CD4⁺ T-helper effector response, i.e. activation of a CD45RO-positive CD4⁺ T-helper cell. This will lead, by virtue of the ‘license to kill’ signal through CD40-triggering of DC (Lanzavecchia, 1998) to a more robust CD8⁺ effector and memory cytotoxic T cell response. In another setting the activated CD4⁺ T-helper cells may activate non-HLA restricted killer cells of the immune system. A Th-cell epitope for which recognition by an HLA class II molecule, or preferably CD4+ activating capability, has been demonstrated experimentally is denominated herein as a confirmed Th-cell epitope.

Preferably, a peptide according to the invention comprises at least one predicted Th-cell epitope from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10 or preferably at least 15 predicted Th-cell epitope(s) as defined herein. Preferably, a peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 predicted Th-cell epitope(s) from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. Even more preferably, a peptide according to the invention comprises or consists of a contiguous amino acid sequence of any of the proteins selected from the group consisting of HBV core protein, HBV polymerase, HBV X protein and HBV large surface protein, wherein said contiguous amino acid sequence comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 predicted Th-cell epitope(s). Preferably, a peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 predicted Th-cell epitope(s) selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466 (see Tables 4b, 5b, 6b, and 7b). More preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 confirmed Th-cell epitope(s) as defined herein. Even more preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 confirmed Th-cell epitope(s) as defined herein and verified using an T helper cell induction assay as described above. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 confirmed Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466.

Preferably, a peptide according to the invention comprises both at least 70 predicted CTL epitopes and at least one predicted Th-cell epitope from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. More preferably, a peptide according to the invention is a peptide derived from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, preferably is a fragment of the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, that comprises at least 70 predicted CTL epitopes, at least one predicted Th-cell epitope and at least 3 proteasomal cleavage sites. The presence of at least 3 proteasomal cleavage sites, at least 70 predicted CTL epitopes and at least 1 Th epitope within a single peptide according to the invention, being a continuous amino acids fragment of an antigen protein of interest, has been observed to be particularly advantageous due to synergy between the Th response and the CTL response in mounting and maintaining an effective CD8⁺ cytotoxic T cell response. Several published studies have demonstrated that CD4⁺ T-helper cells upon interaction with HLA class II epitope presenting dendritic cells (DC) upregulate CD40 ligand. The interaction of the Th-cell by its CD40 ligand with the CD40 molecule on the DC leads to activation of the DC. Activated DCs display upregulated costimulatory molecules and secrete CTL-promoting cytokines. This allows both a more robust CD8⁺ CTL response induced by such an activated DC that presents HLA class I restricted epitopes and a much more robust CTL memory response (Ridge et al., 1998; Schoenberger et al., 1998; Sun et al., 2004). The need for CD40 expression on DC for robust CD8⁺ CTL responses following vaccination with synthetic long peptides (length of 35 aa.) has been demonstrated in Zwaveling et al. (2002).

Accordingly, a preferred peptide according to the invention comprises at least 70 predicted CTL epitopes and at least one predicted Th-cell epitope; preferably at least 70 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least one predicted Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. A more preferred peptide according to the invention comprises at least 70 predicted CTL epitopes and at least 15 predicted Th-cell epitopes; preferably at least 70 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 15 predicted Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-95, 1091-1140, and 1396-1466. More preferably, a peptide according to the invention comprises at least 71, 72, 73, 74, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170 up to 175 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95 up to 96 predicted Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Even more preferably, a peptide according to the invention comprises at least 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170 up to 175 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95 up to 96 predicted Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Preferably, a peptide according to the invention comprises at least 95 predicted CTL epitopes as defined herein and at least 25 predicted Th-cell epitopes as defined herein.

More preferably, a preferred peptide according to the invention comprises at least 5 confirmed CTL epitopes and at least one confirmed Th-cell epitope; preferably at least 5 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least one confirmed Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. A more preferred peptide according to the invention comprises at least 15 confirmed CTL epitopes and at least one confirmed Th-cell epitope; preferably at least 15 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least one confirmed Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-95, 1091-1140, and 1396-1466. More preferably, a peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 confirmed Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Even more preferably, a peptide according to the invention comprises at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 confirmed Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Preferably, a peptide according to the invention comprises at least 15 confirmed CTL epitopes as defined herein and at least 5 confirmed Th-cell epitopes as defined herein.

The HLA class I epitopes in the peptides according to the invention are preferably capable of being presented on HLA molecules being encoded by HLA alleles that are predominant in the population of human subjects to be treated. Preferred HLA class I epitopes in peptides according to the invention are epitopes capable of binding to: HLA-A0101; HLA-A0201; HLA-A0206; HLA-A0301; HLA-A1101; HLA-A2301; HLA-A2402; HLA-A2501; HLA-A2601; HLA-A2902; HLA-A3001; HLA-A3002; HLA-A3101; HLA-A3201; HLA-A3303; HLA-A6801; HLA-A6802; HLA-A7401; HLA-B0702; HLA-B0801; HLA-B1301; HLA-B1302; HLA-B1402; HLA-B1501; HLA-B1502; HLA-B1525; HLA-B1801; HLA-B2702; HLA-B2705; HLA-B3501; HLA-B3503; HLA-B3701; HLA-B3801; HLA-B3901; HLA-B4001; HLA-B4002; HLA-B4402; HLA-B4403; HLA-B4601; HLA-B4801; HLA-B4901; HLA-B5001; HLA-B5101; HLA-B5201; HLA-B5301; HLA-B5501; HLA-B5601; HLA-B5701; HLA-B5801 and HLA-B5802. In a preferred embodiment, a peptide of the invention, covers at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or 100% of the HLA class I molecules that are encoded by HLA alleles predominant in the population of human subjects to be treated, wherein “Cover an HLA class I molecule” is understood herein as comprising a CTL epitope that shows binding affinity, preferably intermediate binding affinity, more preferably high binding affinity to said HLA class I molecule. Preferably, a peptide of the invention covers at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or 100% of group of HLA class I molecules consisting of: HLA-A0101; HLA-A0201; HLA-A0206; HLA-A0301; HLA-A1101; HLA-A2301; HLA-A2402; HLA-A2501; HLA-A2601; HLA-A2902; HLA-A3001; HLA-A3002; HLA-A3101; HLA-A3201; HLA-A3303; HLA-A6801; HLA-A6802; HLA-A7401; HLA-B0702; HLA-B0801; HLA-B1301; HLA-B1302; HLA-B1402; HLA-B1501; HLA-B1502; HLA-B1525; HLA-B1801; HLA-B2702; HLA-B2705; HLA-B3501; HLA-B3503; HLA-B3701; HLA-B3801; HLA-B3901; HLA-B4001; HLA-B4002; HLA-B4402; HLA-B4403; HLA-B4601; HLA-B4801; HLA-B4901; HLA-B5001; HLA-B5101; HLA-B5201; HLA-B5301; HLA-B5501; HLA-B5601; HLA-B5701; HLA-B5801 and HLA-B5802.

The HBV genome (SEQ ID NO: 3; see Table 1) consists of a partially double-stranded circular DNA molecule having four overlapping open reading frames (ORFs) that are responsible for the transcription and expression of seven different hepatitis B proteins through the use of multiple in-frame start codons. The HBV proteins are the core protein and the e antigen (HBeAg) encoded by the C gene, the HBV polymerase encoded by the P gene, the viral surface proteins (small (S), middle (M), and large (L)) encoded by the S gene, and X protein encoded by the X gene. There is an outer shell (or envelope) composed of several proteins known collectively as HBs or surface Proteins. This outer shell is frequently referred to as the surface coat. The outer surface coat surrounds an inner protein shell, composed of HBc protein. This inner shell is referred to as the core particle or capsid. Finally the core particle surrounds the viral DNA and the enzyme DNA polymerase.

The HBV core protein is the major component of the viral nucleocapsid. The amino acid sequences of the HBV polymerase, HBV core protein, HBV X protein and HBV large surface protein are represented by SEQ ID NO: 1, 4, 45 and 1141 respectively (see Table 1).

A preferred amino acid sequence of a human HBV polymerase protein is a sequence having at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 1; a preferred coding sequence is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 2. A preferred amino acid sequence of an HBV core protein is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 4; a preferred coding sequence is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 5. A preferred amino acid sequence of an HBV large surface protein is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 1141, a preferred coding sequence is a sequence having at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 1467.

The full length consensus amino acid sequence of the X protein was obtained by deducing the optimal sequence from the 39 published and reviewed full length (154 amino acid) HBV X protein amino acid sequences in the UniProt database (at: www.uniprot.org). These 39 sequences were first aligned and subsequently for each aa position the most frequently occurring aa was selected for that position in the consensus sequence. The 39 sequences with the following entries were included in the analysis: P69713; P03165; P0C686; P69714; Q8JMY5; Q69604; Q05499; 091531; Q9PX75; P20976; P20975; P20977; P24026; Q9PXA2; Q67923; P0C685; P0C678; O93195; Q9E6S8; P12936; Q91C38; Q913A9; Q8JMY3; Q8JN06; Q8JMZ5; Q69607; Q91B15; Q80IU5; Q4R1S9; Q4R1S1; Q9YZR6; P0C687; Q9QMI3; P0C681; Q80IU8; Q99HR6; P17102; Q67877; and Q69027 (see Table 2). A preferred consensus amino acid sequence of a human HBV X protein is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 45. The consensus amino acid sequence may be encoded by any coding sequence known or designed; the person skilled in the art knows how to design a coding sequence from a known amino acid sequence; such coding sequence may be a codon-optimized sequence. The terms “HBV X protein” and “consensus HBV X protein” are used interchangeably herein.

Percentage of identity is herein determined by calculating the ratio of the number of identical nucleotides/amino acids in the sequence divided by the length of the total nucleotides/amino acids of said sequence, minus the lengths of any gaps. Identity with a given SEQ ID NO means identity based on the full length of said sequence (i.e. over its whole length or as a whole).

Within the context of the present invention, “a peptide derived from an HBV protein” means that the peptide comprises at least 15 and at most 100 consecutive amino acids originating from the HBV core protein, HBV polymerase, HBV X consensus protein and/or HBV large surface protein. In other words, “a peptide derived from the HBV polymerase protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 1, “a peptide derived from the HBV core protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 4, “a peptide derived from the HBV X consensus protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 45, and “a peptide derived from the HBV large surface protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 1141. Preferably, “a peptide derived from the HBV polymerase protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 1, “a peptide derived from the HBV core protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 4, “a peptide derived from the HBV X consensus protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 45, and “a peptide derived from the HBV large surface protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 1141. Therefore, by definition, a peptide according to the invention is distinct from a full length HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, as these full length proteins are all longer than 100 amino acids. Preferably, the peptide of the present invention is from about 15 to about 100 amino acids in length. More preferably the length of the peptide is from 15 up to 100 length indicated herein as the length of the peptide is 15-100 amino acids, or preferably the length of the peptide is 15-95 amino acids, or 15-90 amino acids, or 15-85 amino acids, or 15-70 amino acids, or 15-65 amino acids, or 15-60 amino acids, or 15-55 amino acids, or 15-50 amino acids, even more preferably 15-45 amino acids, even more preferably, 15-40 amino acids, even more preferably 17-39, even more preferably 19-43 amino acids, even more preferably 22-40 amino acids, even more preferably 28-40 and even more preferably 30-39 amino acids. Within the context of the present invention “a peptide which comprises at most 100 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from an HBV protein, preferably being a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X consensus protein and HBV large surface protein and present in a peptide as defined herein, is 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, or 30 amino acids or less. Within the context of the present invention “a peptide which comprises at least 15 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X consensus protein and HBV large surface protein and present in a peptide as defined herein, is at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45 amino acids. Within the context of the present invention “a peptide which comprises 15-100 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X consensus protein and HBV large surface protein and present in a peptide as defined herein, is at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45 amino acids and no more than 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, or 30 amino acids. Within the context of the present invention “a peptide which comprises 15-100 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from a protein selected from the group consisting of SEQ ID NO: 1, 4, 45 and 1141 and present in a peptide as defined herein, is at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45 amino acids and no more than about 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, or 30 amino acids. More preferably, the length of the contiguous amino acid sequence from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein comprised within the peptide is 15-100 amino acids, or preferably 15-95 amino acids, or 15-90 amino acids, or 15-85 amino acids, or 15-70 amino acids, or 15-65 amino acids, or 15-60 amino acids, or 15-55 amino acids, or 15-50 amino acids, even more preferably 15-45 amino acids, even more preferably, 15-40 amino acids, even more preferably 17-39, even more preferably 19-43 amino acids, even more preferably 22-40 amino acids, even more preferably 28-40 and even more preferably 30-39 amino acids. Even more preferably, the length of the contiguous amino acid sequence from the sequences selected from the group consisting of SEQ ID NO: 1, 4, 45 and 1141 comprised within the peptide is 15-100 amino acids, or preferably 15-95 amino acids, or 15-90 amino acids, or 15-85 amino acids, or 15-70 amino acids, or 15-65 amino acids, or 15-60 amino acids, or 15-55 amino acids, or 15-50 amino acids, even more preferably 15-45 amino acids, even more preferably, 15-40 amino acids, even more preferably 17-39, even more preferably 19-43 amino acids, even more preferably 22-40 amino acids, even more preferably 28-40 and even more preferably 30-39 amino acids. A peptide according to the invention may comprise additional amino acids than the ones originating from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein or may entirely be made of or consist of an amino acid sequence originating from a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. A peptide according to the invention may comprise several parts of non-contiguous amino acid sequences from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, wherein it is to be understood that said peptide has a length, a TRIA score and/or amount and type of T cell epitopes as defined herein.

According to one embodiment, a peptide according to the invention consists of any of the contiguous amino acid sequence from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein as defined herein and indicated by its representing SEQ ID NO, whereby it is understood that no amino acids are appended to either end of the said peptide.

According to another embodiment, the peptide according to the invention comprises any of the contiguous amino acid sequences from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein as defined herein and indicated by its representing SEQ ID NO and further may comprise a modified amino acid and/or a covalently linked functional group such as a fluorinated group, a human toll-like receptor ligand and/or agonist, an oligonucleotide conjugate, PSA, a sugar chains or glycan, a pam3cys and/or derivative thereof, preferably a pam3cys lipopeptide or variant or derivative thereof, preferably such as described in WO2013051936A1, CpG oligodeoxynucleotides (CpG-ODNs), Cyclic dinucleotides (CDNs), 2-aminoisobutyric acid (Abu), Muramyl dipeptide (MDP), a DC pulse cassette, a tetanus toxin derived peptide.

In an embodiment, the peptide of the invention comprises or consists of a non-naturally occurring sequence as a result of the synthesis of non-natural lengths or as a result of comprising additional amino acids not originating from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein or as a result of comprising non-contiguous amino acid sequences from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, and/or as a result of comprising a modified amino acid and/or a non-naturally occurring amino acid and/or a covalently linked functional group such as a fluorinated group, a fluorcarbon group, a human toll-like receptor ligand and/or agonist, an oligonucleotide conjugate, PSA, a sugar chains or glycan, a pam3cys and/or derivative thereof preferably such as described in WO2013051936A1, CpG oligodeoxynucleotides (CpG-ODNs), Cyclic dinucleotides (CDNs), a DC pulse cassette, a tetanus toxin derived peptide, a human HMGB1 derived peptide; either within the peptide or appended to the peptide, as indicated above. The peptide of the invention may comprise 2-aminoisobutyric acid (Abu, an isostereomer of cysteine). A cysteine of the peptide of the invention may be replaced by Abu. Encompassed within the present invention is a peptide of SEQ ID NO: 77, wherein the N-terminal cysteine has been replaced by Abu.

Preferably, a peptide of the invention is an isolated peptide, wherein “isolated” does not reflect the extent to which the peptide is purified, but indicates that the peptide has been removed from its natural milieu (i.e., that has been subject to human manupilation), and may be a recombinantly produced peptide or a synthetically produced peptide.

Preferably, the invention relates to a peptide that can be effectively used in the prevention, partial clearance and/or treatment or full clearance of a HBV related disease or condition in a subject, preferably as detectable by:

-   -   an activation or an induction of the immune system and/or an         increase in HBV specific activated CD4⁺ and/or CD8⁺ T-cells in         peripheral blood or an increase of the cytokines produced by         these T-cells after at least one week of treatment; and/or     -   an inhibition of proliferation of HBV infection or a detectable         decrease of HBV infected cells or a decrease in cell viability         of HBV infected cells; and/or     -   an induction or increased induction of HBV infected cell death;         and/or     -   an inhibition or prevention of the increase of HBV infected         cells.

In all embodiments of the present invention, a subject is preferably a mammal, more preferably a human. A subject may be an animal model, preferably a non-human mammalian model with humanized HLA class I and class II molecules, or a mammalian, preferably human, organ, such as a liver.

In all embodiments of the present invention, the term “HBV related disease or condition” is preferably defined as acute HBV infection, chronic HBV infection and other conditions where the hepatitis virus is found in the blood or body fluids containing blood of a subject, such as liver cirrhosis and liver cancer, or optionally of an asymptomatic subject that is characterized by the presence of the virus in the body of said subject.

In the context of the invention, a patient may survive and may be considered as being disease free as a consequence of treatment according to the invention. Alternatively, the disease or condition may have been stopped or regressed (i.e. cleared or partially cleared infection). A significant increase of HBV-specific activated CD4⁺ or CD8⁺ cells in peripheral blood at least one week after vaccination is preferably at least a 5%, 10%, 20%, 30% increase or more. An inhibition of the proliferation of HBV infected cells is preferably at least 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75% inhibition or more. An induction of HBV infected cell death may be at least 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, or more. HBV infection may be inhibited at least 5%, 10%, 20%, 30%, 40%, 50%, 55%, 60%, 65%, 70% or 75% induction, or more. HBV infected cells may be reduced by at least 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98% or 100%.

In each embodiment, within this or further aspects disclosed herein, wherein the effect of a peptide according to the invention, a composition according to the invention, a polynucleotide according to the invention, a viral vector comprising a polynucleotide according to the invention and/or a cell according to the invention and/or a cell obtained or obtainable by a method according to the invention, is quantified, the assay may be carried out by comparison to a subject not treated or to the same subject before treatment.

Acute and chronic HBV infection can be treated using the present invention. A peptide according to the invention comprising epitopes which are to be presented to T-cell receptors of CD8⁺ cytotoxic T cells and/or CD4⁺ T-helper cells preferably fulfill a number of structural requirements as defined herein. In vitro and ex vivo T cell experiments are preferably used to confirm the capability of peptides according to the invention to induce substantial CD4⁺ T-helper and CD8⁺ cytotoxic T cell responses. The peptides of the present invention thereby provide a marked improvement in the selection of relatively short peptides that may be chemically synthesized, comprising the most potent and most widely applicable HLA class I and/or class II presented T cell epitopes derived from HBV.

In an embodiment, a peptide is distinct from a contiguous sequence of amino acids of HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein.

A peptide according to the invention comprising a T-cell epitope from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, may be modified by deletion or substitution of one or more amino acids, by extension at the N- and/or C-terminus with additional amino acids or functional groups, which may improve bio-availability, targeting to T-cells, or comprise or release immune modulating substances that provide adjuvant or (co) stimulatory functions. The optional additional amino acids at the N- and/or C-terminus are preferably not present in the corresponding positions in the native amino acid sequence of HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein.

A peptide according to the invention comprising a T-cell epitope is obtainable by chemical synthesis and subsequent purification according to methods well-known in the art. (see e.g. Atherton et al., 1989; Barany et al., 1979; Fields et al., 1997). A peptide according to the invention is preferably soluble in physiologically acceptable watery solutions (e.g. PBS) comprising no more than 35, 20, 10, 5 or 0% DMSO. In such a solution the peptide according to the invention is preferably soluble at a concentration of at least 0.5, 1, 2, 4, or 8 mg peptide per ml. More preferably, a mixture of more than one different peptide according to the invention is soluble at a concentration of at least 0.5, 1, 2, 4, or 8 mg peptide per ml in such solutions.

The peptides according to the invention may be easily synthesized and are large enough to be taken up by professional antigen presenting cells, in particular dendritic cells (DC), processed by the proteasome and/or the endosomal/lysosomal degradation and antigen processing system and preferably have sufficient length to contain at least 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 73, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170 to preferably up to 175 CTL epitopes and/or at least 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 to preferably up to 96 Th-cell epitopes as defined herein. Optionally, a peptide according to the invention may comprise N- or C-terminal extensions, which may be amino acids, modified amino acids or other functional groups that may for instance enhance bio-availability, cellular uptake, processing and/or solubility.

Preferably, a peptide according to the invention is a peptide comprising a peptide with an amino acid sequence selected from the group consisting of:

-   -   a fragment of 15 to 30 amino acids of SEQ ID NO: 51, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 52, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 53, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 54, preferably         contiguous amino acids,     -   a fragment of 15 to 39 amino acids of SEQ ID NO: 55, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 56, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 57, preferably         contiguous amino acids,     -   a fragment of 15 to 32 amino acids of SEQ ID NO: 58, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 59, preferably         contiguous amino acids,     -   a fragment of 15 to 38 amino acids of SEQ ID NO: 60, preferably         contiguous amino acids,     -   a fragment of 15 to 38 amino acids of SEQ ID NO: 61, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 62, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 63, preferably         contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 64, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 65, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 66, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 67, preferably         contiguous amino acids,     -   a fragment of 15 to 39 amino acids of SEQ ID NO: 68, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 69, preferably         contiguous amino acids,     -   a fragment of 15 to 32 amino acids of SEQ ID NO: 70, preferably         contiguous amino acids,     -   a fragment of 15 to 38 amino acids of SEQ ID NO: 71, preferably         contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 72, preferably         contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 73, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 74, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 75, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 76, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 77, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 78, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 79, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 1142,         preferably contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 1143,         preferably contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 1144,         preferably contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 1145,         preferably contiguous amino acids,     -   a fragment of 15 to 32 amino acids of SEQ ID NO: 1468,         preferably contiguous amino acids,     -   a fragment of 15 to 31 amino acids of SEQ ID NO: 1469,         preferably contiguous amino acids,     -   a fragment of 15 to 30 amino acids of SEQ ID NO: 1470,         preferably contiguous amino acids,     -   a fragment of 15 to 31 amino acids of SEQ ID NO: 1471,         preferably contiguous amino acids, and;

wherein the length of the preferably contiguous amino acid sequence is preferably at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 or 33 amino acids and/or preferably no more than 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21, 20, 19, 18, 17, 16, 15 amino acids, most preferably a length of 30-39 amino acids.

In a second aspect, the invention provides a polynucleotide encoding a peptide according to the invention, preferably a peptide as defined herein above. A polynucleotide may be any polynucleotide comprising e.g. RNA, DNA, and/or cDNA; a polynucleotide may be single stranded or double stranded and may comprise nucleotide analogues and/or nucleotide equivalents such as a peptide nucleic acid (PNA) and a morpholino nucleotide analogue. A polynucleotide may be codon optimized for a host of choice to facilitate expression of the encoded subject matter.

The polynucleotide according to the invention does not encode a wild-type full length HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, but rather encode a peptide according to the invention as such, or flanked by amino acid sequence that are not contiguous with a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. Such flanking amino acids may be from proteins other than a wild-type HBV and/or they may be from other locations within a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein that are not contiguous with the peptide they flank. Preferably, the polynucleotide encodes two or more peptides according to the invention arranged as beads-on-string, whereby the peptides according to the invention (the beads) are linked directly together and/or are linked through linker sequences that are from proteins other than a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, and/or from other locations within a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, that are not contiguous with the peptide they flank. The amino acid sequences flanking or linking the peptides may comprise proteolytic cleavage sites. A polynucleotide according to the invention may be applied to deliver a peptide according to the invention in various ways. A polynucleotide according to the invention may e.g. be used in the production of recombinant protein or peptide in a suitable host cell (e.g. a bacterial host cell such as E. coli, a suitable yeast host cell such as S. cerevisiae, a suitable filamentous fungal such as an Aspergillus or mammalian host cell) from which the recombinant protein or peptide may be purified. Alternatively the polynucleotide may be operably linked to expression regulatory sequences (promoters and the like) and incorporated in an expression construct for human cells. Such (autologous) cells may be transfected or transduced ex vivo to be (re)-administered to a subject in need thereof. Alternatively such expression construct according to the invention may be incorporated into a suitable gene therapy vector. Viral vectors (based on a defective virus) are more efficient agents for gene transfer as compared to non-viral agents. Suitable viral expression constructs include e.g. vectors that are based on adenovirus, adeno-associated virus (AAV), retroviruses or modified vaccinia Ankara (MVA). The polynucleotide according to the invention may also be operably linked to a sequence encoding and adjuvant such as a Toll-like receptor (TLR) ligand, a NOD ligand, or a RIG-I ligand.

In a third aspect, the present invention provides a cell comprising the polynucleotide according to the second aspect of the invention. Such cell can be used for e.g. production of a peptide according to the invention or for medical purposes such as prevention and/or treatment of an HBV related disease as defined elsewhere herein. Said cell may be any host cell. For the specific applications such as described here above, the selection of the host cell may be made according to such use. The host cell may be a prokaryote or may be a eukaryote. A preferred prokaryote cell is E. coli. When the cell is a eukaryote, the cell preferably is a mammalian, insect, plant, fungal, or algal cell. Preferred mammalian cells include e.g. Chinese hamster ovary (CHO) cells, COS cells, 293 cells, PerC6 cells, and antigen presenting cells such as dendritic cells. Preferred insect cells include e.g. Sf9 and Sf21 cells and derivatives thereof. Preferred fungal cells include Candida, Hansenula, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces, Yarrowia and filamentous fungal cells. Most preferably, the eukaryotic cell is a human antigen presenting cell, preferably a dendritic cell.

Methods to introduce a polynucleotide into a cell are known to the person skilled in the art. When expression of the polynucleotide is desired, the person skilled in the art knows how to achieve such; the polynucleotide may e.g. be provided with proper control sequences such as a promoter and terminator sequence and may be inserted into a proper vector such as a plasmid or a method described in the second aspect of the invention may be used.

The present invention also provides for an antigen presenting cell such as a dendritic cell as defined earlier herein that has been contacted and/or loaded with a peptide according to the invention, preferably a peptide according to the first aspect of the present invention. Such preferably autologous dendritic cell may be used for immune therapeutic treatment of a subject in need thereof. Such dendritic cell can be isolated from the subject, loaded with at least one peptide according to the invention and used for treatment.

In a fourth aspect, the present invention provides a method for the preparation of an HBV specific T-cell, said method comprising contacting a T-cell with an antigen presenting cell expressing a polynucleotide according to the invention and/or contacting a T-cell with an antigen presenting cell loaded with a peptide according to the invention; and, optionally, culturing said T-cell. The T-cell is preferably a CD8⁺ cytotoxic T-cell or a CD4⁺ T-helper cell.

Contacting a cell with a polynucleotide may be performed using any method known to the person skilled in the art, preferably a polynucleotide according to the invention is introduced into the antigen presenting cell (APC), preferably a dendritic cell, using transfection. Before contacting, the polynucleotide according to the invention may be provided with proper control sequences, or be comprised into a proper vector such as described elsewhere herein.

Contacting a T-cell with a peptide according to the invention can be performed by any method known to the person skilled in the art. Preferably, a peptide or an epitope comprised in a peptide is presented to the CD8⁺ cytotoxic T-cell or CD4⁺ T-helper cell by an HLA class I or an HLA class II molecule on the surface of an antigen presenting cell, preferably a dendritic cell. The person skilled in the art knows how to load an antigen presenting cell with a peptide.

Culturing said T-cell may be performed using any method known by the person skilled in the art. Maintaining a T-cell under conditions to keep the cell alive is herein also to be construed to be culturing.

Preferably, the T-cell according to this aspect of the invention is contacted with a peptide according to the invention as defined in the first aspect of the invention.

In a fifth aspect, the present invention provides a T-cell obtainable by the method depicted in the fourth aspect of the present invention. Preferably, such T-cell is a T-cell that is obtained by the method according to the fourth aspect of the invention. The T-cell is preferably a CD8⁺ cytotoxic T-cell or a CD4⁺ T-helper cell.

Preferably, the T-cell according to this aspect of the invention has been contacted with a peptide according to the invention as defined in the first aspect of the invention.

In a sixth aspect, the present invention provides a composition useful for the prevention and/or treatment of an HBV related disease or related condition, comprising a peptide according to the invention and/or a polynucleotide according to the invention and/or a cell, preferably a T-cell, according to the invention and/or a cell, preferably a T-cell, obtained by the method according to the fourth aspect of the invention and a pharmaceutically acceptable carrier.

When comprising a peptide according to the invention, the composition according to the invention preferably comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different peptides according to the invention. Preferably, a composition according to the invention comprises a peptide according to the invention as defined in the first aspect of the invention. In a preferred embodiment, a composition of the invention comprises a combination of peptides wherein said combination of peptides covers at least 70%, 80%, 90%, 92%, 94%, 95%, 96%, 97%, 98%, 99% or 100% of the HLA class I molecules that are encoded by HLA alleles predominant in the population of human subjects to be treated as defined herein above.

When comprising a polynucleotide according to the present invention, the composition according to the invention preferably comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different polynucleotides according to the invention. Preferably, a composition according to the invention comprises a polynucleotide according to the invention as defined in the second aspect of the invention.

When comprising a cell according to the invention, the composition according to the invention preferably comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different cells, preferably T-cells that have been contacted with a peptide according to the invention. Preferably, said T-cells have been contacted with a peptide according to the invention as defined in the first aspect of the invention. The T-cell is preferably a CD8⁺ cytotoxic T-cell or a CD4⁺ T-helper cell.

In a preferred embodiment, the composition of the invention comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different peptides of the peptides consisting of or comprising of a peptide selected from the group consisting of SEQ ID NO: 51-79, 1142-1145 and 1468-1471, more preferably selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 76, 77, 1142 and 1469, more preferably selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 77, 1142 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 76, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 60, 63, 71, 74, 75 and 1469, most preferably selected from the group of SEQ ID NO: 75, 1469 and 63. Further preferred is a composition that comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different peptides of the peptides consisting of or comprising of a peptide selected from the group consisting of SEQ ID NO: 51, 60, 63, 64, 68, 71, 74-77, more preferably selected from the group consisting of SEQ ID NO: 63, 71 and 75.

In a preferred embodiment, the composition of the invention comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63 and peptide that comprises or consists of a peptide of SEQ ID NO: 1143.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1143 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 71 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 71 and peptide that comprises or consists of a peptide of SEQ ID NO: 63.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1144 and peptide that comprises or consists of a peptide of SEQ ID NO: 63.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1144 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1144 and peptide that comprises or consists of a peptide of SEQ ID NO: 1143.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63, a peptide that comprises or consists of a peptide of SEQ ID NO: 1143, and a peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63, a peptide that comprises or consists of a peptide of SEQ ID NO: 1143, a peptide that comprises or consists of a peptide of SEQ ID NO: 75, and a peptide that comprises or consists of a peptide of SEQ ID NO: 1144.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 75, and a peptide that comprises or consists of a peptide of SEQ ID NO: 1469. Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63, and a peptide that comprises or consists of a peptide of SEQ ID NO: 1469.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 75, a peptide that comprises or consists of a peptide of SEQ ID NO: 1469, and a peptide that comprises or consists of a peptide of SEQ ID NO: 63. Preferably, said composition further comprising a peptide that comprises or consists of a peptide of SEQ ID NO: 60 and/or that comprises or consists of a peptide of SEQ ID NO: 71, and/or that comprises or consists of a peptide of SEQ ID NO: 74.

A preferred composition of the invention comprises a peptide that consists of or comprises a peptide of SEQ ID NO: 75, a peptide that consists of or comprises a peptide of SEQ ID NO: 63, and a peptide that consists of or comprises a peptide of SEQ ID NO: 1469

A preferred composition of the invention comprises a peptide that consists of or comprises a peptide of SEQ ID NO: 75, a peptide that consists of or comprises a peptide of SEQ ID NO: 63, and a peptide that consists of or comprises a peptide of SEQ ID NO:

71.

A pharmaceutically acceptable carrier can be any such carrier known to the person skilled in the art, e.g. buffered aqueous solutions at physiological ionic strength and/or osmolarity (such as e.g. PBS).

Preferably, a composition according to the present invention further comprises at least one adjuvant. Such adjuvant may be any adjuvant known to the person skilled in the art. Preferred adjuvants are defined later herein.

A preferred use of a peptide, polynucleotide, composition, cell and/or T-cell according to the invention or a T-cell obtainable or obtained by a method according to the invention is the use as a medicament. A specific preferred use of a peptide, polynucleotide, composition, cell and/or T-cell according to the invention or a T-cell obtainable or obtained by a method according to the invention is for the treatment and/or prevention of an HBV related disease or condition. Accordingly, the invention provides for the use of a peptide, polynucleotide, composition, cell and/or T-cell according to the invention or a T-cell obtainable or obtained by a method according to the invention for the manufacturing of a medicament for the treatment and/or prevention of an HBV related disease.

The invention further provides a method for the prevention and/or treatment of an HBV related disease or condition comprising administering to a subject an effective amount of a peptide, polynucleotide, composition, cell or T-cell according to the invention and/or a T-cell obtainable or obtained by a method according to the invention.

Formulation of medicaments, ways of administration and the use of pharmaceutically acceptable excipients are known and customary in the art and for instance described in Remington; The Science and Practice of Pharmacy, 21^(st) Edition 2005, University of Sciences in Philadelphia. Pharmaceutical compositions and medicaments according to the invention are preferably formulated to be suitable for intravenous or subcutaneous, or intramuscular administration, although other administration routes can be envisaged, such as mucosal administration or intradermal and/or intracutaneous administration, e.g. by injection. Intradermal administration is preferred herein. Advantages and/or preferred embodiments that are specifically associated with intradermal administration are later on defined in a separate section entitled “intradermal administration”.

It is furthermore encompassed by the present invention that the administration of a peptide, a polynucleotide, a composition and/or a cell according to the invention and/or a cell obtainable or obtained by a method according to the invention with an appropriate pharmaceutical excipient such as an adjuvant and/or a carrier may be carried out as a single administration. Alternatively, the administration may be repeated if needed and/or distinct peptides, polynucleotides, compositions and/or cells according to the invention and/or cells obtainable or obtained by a method according to the invention with appropriate pharmaceutical excipients such as adjuvants and/or carriers, may be sequentially administered.

The peptide, polynucleotide, composition and/or cell according to the invention and/or cell obtainable or obtained by a method according to the invention (also referred to as medicaments according to the invention) may preferably comprise at least one immune response stimulating compound or adjuvant. Advantageously the medicaments according to the invention may additionally comprise one or more synthetic adjuvants. Such adjuvant may be admixed to the medicament according to the invention or may be administered separately to the subject, mammal or human, to be treated. Particularly preferred are those adjuvants that are known to act via the Toll-like receptors and/or via a RIG-I (Retinoic acid-Inducible Gene-1) protein and/or via an endothelin receptor. Immune modifying compounds that are capable of activation of the innate immune system can be activated particularly well via Toll like receptors (TLRs), including TLRs 1-10. Compounds capable of activating TLR receptors and modifications and derivatives thereof are well documented in the art. TLR1 may be activated by bacterial lipoproteins and acetylated forms thereof, TLR2 may in addition be activated by Gram positive bacterial glycolipids, LPS, LPA, LTA, fimbriae, outer membrane proteins, heat shock proteins from bacteria or from the host, and Mycobacterial lipoarabinomannans. TLR3 may be activated by dsRNA, in particular of viral origin, or by the chemical compound poly(I:C). TLR4 may be activated by Gram negative LPS, LTA, Heat shock proteins from the host or from bacterial origin, viral coat or envelope proteins, taxol or derivatives thereof, hyaluronan containing oligosaccharides and fibronectins. TLR5 may be activated with bacterial flagellae or flagellin. TLR6 may be activated by mycobacterial lipoproteins and group B Streptococcus heat labile soluble factor (GB S-F) or Staphylococcus modulins. TLR7 may be activated by imidazoquinolines, such as imiquimod, resiquimod and derivatives imiquimod or resiquimod. TLR9 may be activated by unmethylated CpG DNA or chromatin—IgG complexes. In particular TLR3, TLR7 and TLR9 play an important role in mediating an innate immune response against viral infections, and compounds capable of activating these receptors are particularly preferred for use in the methods of treatment and in the compositions or medicaments according to the invention. Particularly preferred adjuvants comprise, but are not limited to, synthetically produced compounds comprising dsRNA, poly(I:C), unmethylated CpG DNA which trigger TLR3 and TLR9 receptors, IC31, a TLR 9 agonist, IMSAVAC, a TLR 4 agonist, Montanide ISA-51, Montanide ISA 720 (an adjuvant produced by Seppic 7, France). RIG-I protein is known to be activated by ds-RNA just like TLR3 (Kato et al, 2005). A particularly preferred TLR ligand is a pam3cys and/or derivative thereof, preferably a pam3cys lipopeptide or variant or derivative thereof, preferably such as described in WO2013051936A1. Further preferred adjuvants are Cyclic dinucleotides (CDNs), Muramyl dipeptide (MDP) and poly-ICLC. In a preferred embodiment, the adjuvants of the invention are non-naturally occurring adjuvants such as the pam3cys lipopeptide derivative as described in WO2013051936A1, Poly-ICLC, imidazoquinoline such as imiquimod, resiquimod or derivatives thereof, CpG oligodeoxynucleotides (CpG-ODNs) having a non-naturally occurring sequence, and peptide-based adjuvants, such as muramyl dipeptide (MDP) or tetanus toxoid peptide, comprising non-naturally occurring amino acids.

In another preferred embodiment, the synthetic adjuvant compounds are physically linked to the peptides of the invention. Physical linkage of adjuvants and costimulatory compounds or functional groups to the HLA class I and HLA class II epitope comprising peptides provides an enhanced immune response by improved targeting to antigen-presenting cells, in particular dendritic cells, that internalize, metabolize and display antigen and by simultaneously stimulating such cells to up-regulate expression of a variety of co-stimulatory molecules, thereby becoming efficient T cell response inducing and enhancing cells. Another preferred immune modifying compound is an inhibitor of an endothelin receptor such as BQ-788 (Buckanovich R J et al., 2008; Ishikawa K, 1994). BQ-788 is N-cis-2,6-dimethylpiperidinocarbonyl-L-gamma-methylleucyl-D-1-methoxycarbonyltryptophanyl-D-norleucine. However any derivative of BQ-788 or modified BQ-788 compound is also encompassed within the scope of this invention. Another preferred immune response stimulating compound or adjuvant is Interferon alpha (IFNα), more preferably pegylated Interferon alpha, which may be admixed to the medicament according to the invention, or may be administered separately to the subject as an immuno-modulatory agent. It is to be construed herein that when an immune response stimulating compound is admixed to the medicament according to the invention, it is depicted as an adjuvant; when administered separately, it is depicted as an immuno-modulatory agent, or an immuno-modulator, which terms are used herein interchangeably. Furthermore, the use of antigen presenting cell (co)stimulatory molecules, as set out in WO99/61065 and in WO03/084999, in combination with the peptides and compositions of the invention is preferred. In particular the use of 4-1BB and/or CD40 ligands, agonistic antibodies, OX40 ligands, CD27 ligands or functional fragments and derivatives thereof, as well as synthetic compounds with similar agonistic activity are preferably administered separately or combined with the peptides of the invention to subjects to be treated in order to further stimulate the mounting of an optimal immune response in the subject.

In addition, a preferred embodiment comprises delivery of the medicaments according to the invention, with or without additional immune stimulants such as TLR ligands and/or anti CD40/anti-4-1BB/anti-OX-40 or anti-CD27 antibodies in a slow release vehicle such as mineral oil (e.g. Montanide ISA 51) or PLGA. Alternatively, the medicament according to the invention may be delivered intradermally, e.g. by injection, with or without immune stimulants (adjuvants and/or immuno-modulators). Preferably, for intradermal delivery the medicaments according to the invention are administered in a composition consisting of the medicaments and one or more immunologically inert pharmaceutically acceptable carriers, e.g. buffered aqueous solutions at physiological ionic strength and/or osmolarity (such as e.g. PBS).

In a preferred embodiment, a medicament according to the invention as defined herein is formulated to be suitable for intradermal administration or application. Intradermal is known to the skilled person. In the context of the invention, intradermal is synonymous with intradermal and is distinct from subcutaneous. A most superficial application of a substance is epicutaneous (on the skin), then would come an intradermal application (in or into the skin), then a subcutaneous application (in the tissues just under the skin), then an intramuscular application (into the body of the muscle). An intradermal application is usually given by injection. An intradermal injection of a substance can be done to test a possible reaction, allergy and/or cellular immunity to it, but can also be performed to elicit a specific antibody or T cell immune response. A subcutaneous application is usually also given by injection: a needle is injected in the tissues under the skin.

The advantage of intradermal administration is that the formulation procedure can be simplified and be made more robust. Furthermore, intradermal vaccine delivery has been repeatedly shown to allow significant dose sparing for eliciting vaccine-induced antibody or T cell responses when compared to conventional administration methods such as intramuscular and subcutaneous administration. This effect is attributed to the relatively dense network of immune cells present in the skin. This was also shown with the HPV16 synthetic long peptides in a human study published by Van der Burg et al. (2007). In this study it was shown that intradermal injection of pools of HPV16 synthetic long peptides is safe and results in the migration of HPV16-specific T cells into the skin as well as in an increase in the number of HPV16-specific T cells circulating in the blood.

In an embodiment, a medicament according to the invention does not comprise any adjuvant such as Montanide ISA-51, and specifically Montanide ISA-51. This means that the formulation of the medicament is more simple: an oil-water based emulsion is preferably also not present in a medicament according to the invention. Accordingly, a medicament according to the invention preferably does not comprise an adjuvant such as Montanide ISA-51 and specifically Montanide ISA-51 and/or does not comprise an oil-in-water based emulsion; more preferably a medicament according to the invention comprises neither of these to adjuvant and even more preferably comprises no adjuvant at all. Therefore, in an embodiment, the medicament according to the invention is a, preferably buffered, aqueous solution, preferably at physiological ionic strength and/or osmolality, such as e.g. PBS (Phosphate Buffer Saline) or water for injection (WFI), comprising or consisting of one or more medicaments as defined earlier herein. The skilled person knows how to prepare such a solution.

A medicament according to the invention has another advantage, which is that by intradermally administering low amounts of a medicament, preferably a peptide as earlier herein defined, an immunogenic effect may still be achieved. The amount of each peptide used is preferably ranged from 1 and 1000 μg, more preferably from 5 and 500 μg, even more preferably from 10 and 100 μg.

In an embodiment, the medicament according to the invention comprises a peptide as earlier defined herein and at least one adjuvant, said adjuvant being not formulated in an oil-in water based emulsion and/or not being of an oil-in-water emulsion type as earlier defined herein. This type of medicament according to the invention may be administered as a single administration. Alternatively, the administration of a peptide as earlier herein defined and/or an adjuvant may be repeated if needed and/or distinct peptides and/or distinct adjuvants may be sequentially administered. It is further encompassed by the present invention that a peptide according to the invention is administered intradermally whereas an adjuvant as defined herein is sequentially administered. The adjuvant may be intradermally administered. However any other way of administration may be used for the adjuvant. Intradermal administration of a peptide may be attractive since typically and depending on the disease, the injection of the vaccine is realized at or as close by as possible to the site of the disease resulting in the local activation of the disease draining lymph node, resulting in a stronger local activation of the immune system. A preferred immune response stimulating compound (immuno-modulator) or adjuvant for intradermal administration is Interferon alpha (IFNα), more preferably pegylated Interferon alpha, which may be admixed to the medicament according to the invention, or may be administered separately, for example by subcutaneous injection to the subject. When administered separately the Interferon alpha is preferably also administered subcutaneously and is preferably administered at a dose of 1 microgram/kilogram of body weight within 10 cm proximity to the site where the medicament according to the invention is administered, such described in Zeestraten et al, 2013.

Another typical advantage of the medicaments according to the invention is that relatively low amounts of peptides may be used, in one single shot, in a simple formulation and without any adjuvant known to give undesired side-effects as Montanide ISA-51.

The medicament for intradermal administration may be any medicament according to the invention as defined herein. A medicament according to the invention used for subcutaneous administration may be the same as the one used for intradermal administration and may thus be any medicament according to the invention as defined herein. The skilled person knows how to formulate a medicament suited for subcutaneous administration.

Preferably, a medicament according to the invention for subcutaneous administration comprises a peptide as already herein defined in combination with an adjuvant. Preferred adjuvants or immune modulators have already been mentioned herein. Other preferred adjuvants are of the type of an oil-in water emulsions such as incomplete Freund's adjuvant or IFA, Montanide ISA-51 or Montanide ISA 720 (Seppic France). In a further preferred embodiment, a medicament according to the invention suited for subcutaneous administration comprises one or more peptides according to the invention, an adjuvant or immune modulator as earlier defined herein and an inert pharmaceutically acceptable carrier and/or excipients all as earlier defined herein. Formulation of medicaments, and the use of pharmaceutically acceptable excipients are known and customary in the art and for instance described in Remington; The Science and Practice of Pharmacy, 21^(st) Edition 2005, University of Sciences in Philadelphia. A preferred immune response stimulating compound or adjuvant for subcutaneous administration is Interferon alpha (IFNα), more preferably pegylated Interferon alpha, which may be admixed to the medicament according to the invention, or may be administered separately to the subject. When administered separately, the Interferon alpha is preferably also administered subcutaneously and is preferably administered at a dose of 1 microgram/kilogram of body weight within 10 cm proximity to the site where the medicament according to the invention is administered, such described in Zeestraten et al., 2013.

In an embodiment, the medicament according to the invention suited for intradermal administration may be simultaneously administered with a medicament according to the invention suited for subcutaneous administration. Alternatively, both medicaments may be sequentially intradermally and subsequently subcutaneously administered or vice versa (first subcutaneous administration followed by intradermal administration). In this embodiment as in the earlier described embodiment dedicated to the intradermal administration, the intradermal and/or subcutaneous administration of a medicament according to the invention, preferably a peptide according to the invention, and/or of an adjuvant may be repeated if needed and/or of distinct medicament, preferably peptides and/or of distinct adjuvants may be sequentially intradermally and/or subcutaneously administered. It is further encompassed by the present invention that a medicament according to the invention, preferably a peptide is administered intradermally and/or subcutaneously whereas an adjuvant as defined herein is sequentially administered as immune-modulator. The adjuvant or immune-modulator may be intradermally and/or subcutaneously administered. However any other way of administration may be used for the adjuvant or immune-modulator.

We expect the combination of an intradermal and a subcutaneous administration of a medicament according to the invention is advantageous. DC in the epidermis are clearly different from DC in the dermis and in the subcutis. The intracutaneous (intradermal) immunization will cause antigen processing and activation of epidermal DC (Langerin-positive Langerhans cells) that through their dendritic network are in close contact with the keratinocytes. This will also optimally activate inflammatory pathways in the interactions between Langerhans cell and keratinocytes, followed by trafficking of antigen loaded and activated Langerhans cell to the skin-draining lymph nodes. The subcutaneous administration will activate other DC subsets, that will also become loaded with antigen and travel independently to the skin-draining lymph nodes. Conceivably, the use of a medicament which may be administered both intradermally and subcutaneously may lead to a synergistic stimulation of T-cells in these draining nodes by the different DC sub sets.

A medicament according to the present invention and the methods of treatment described herein using a medicament according to the invention may advantageously be combined with other medicaments and methods of treatment. As such, a medicament according to the invention or a method of treatment according to the invention may be combined with e.g. therapy, and/or antibody therapy against an HBV related disease or may be combined with e.g. immunotherapy and/or antibody therapy against another than HBV related disease, or may be combined with immunotherapy against another antigen than HBV to treat an HBV related disease.

In this document and in its claims, the verb “to comprise” and its conjugations is used in its non-limiting sense to mean that items following the word are included, but items not specifically mentioned are not excluded. In addition, reference to an element by the indefinite article “a” or “an” does not exclude the possibility that more than one of the element is present, unless the context clearly requires that there be one and only one of the elements. The indefinite article “a” or “an” thus usually means “at least one”. The word “about” or “approximately” when used in association with a numerical value (e.g. about 10) preferably means that the value may be the given value (of 10) more or less 0.1% of the value.

The sequence information as provided herein should not be so narrowly construed as to require inclusion of erroneously identified bases. The skilled person is capable of identifying such erroneously identified bases and knows how to correct for such errors. In case of sequence errors, the sequence of the HBV core, HBV polymerase and HBV large surface protein polypeptides obtainable by expression of the gene present in SEQ ID NO: 5, 2 and 1467 containing the respective nucleic acid sequence coding for the polypeptides should prevail.

All patent and literature references cited in the present specification are hereby incorporated by reference in their entirety.

Unless stated otherwise, the practice of the invention will employ standard conventional methods of molecular biology, virology, microbiology or biochemistry. Such techniques are described in Sambrook et al. (1989) Molecular Cloning, A Laboratory Manual (2^(nd) edition), Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press; in Sambrook and Russell (2001) Molecular Cloning: A Laboratory Manual, Third Edition, Cold Spring Harbor Laboratory Press, NY; in Volumes 1 and 2 of Ausubel et al. (1994) Current Protocols in Molecular Biology, Current Protocols, USA; and in Volumes I and II of Brown (1998) Molecular Biology LabFax, Second Edition, Academic Press (UK); Oligonucleotide Synthesis (N. Gait editor); Nucleic Acid Hybridization (Hames and Higgins, eds.).

BRIEF DESCRIPTION OF THE DRAWINGS

FIGS. 1A-1D: Proteasome-mediated cleavage pattern of long vaccine peptides as predicted in silico and observed in experimental in vitro digestions. For each SLP, the observed cleavage sites are indicated by arrows (major and minor cleavage sites are indicated by bold and thin arrows, respectively, as further detailed herein). Further, for each of the ten SLPs tested in the digestion experiments (SLP1, SLP10 and SLP21 in FIG. 1A; SLP14, SLP18 and SLP21 in FIG. 1B; SLP24, SLP25 and SLP26 in FIG. 1C; and SLP 27 in FIG. 1D), the predicted C-score is indicated in the first row, the confirmed predicted cleavage sites are indicated in the second row (indicated as ‘+’), the amino acid position within the source protein is indicated in the third row, the respective amino acids in the sequence are indicated in the fourth row, and the amino acid number within the SLP is indicated in the fifth row. For SLP27, C* indicates the cysteine replacement by Abu.

FIG. 2: Overview of responding naïve donors after T cell induction with HBV-derived long peptides. Combined data of IFNγ production as measured by ELISA (‘ELISA’); hatched box SI (Stimulation Index)>1.5, and T cell proliferation (‘Prolif’) as measured by 3H thymidine incorporation; hatched box SI>1.5. N.t.: not tested

FIG. 3: Overview of responding HBV-immune donors after stimulation with HBV-derived long peptides. Data represent IFNγ-ELISpot results, with hatched boxes indicating a positive response with SI (Stimulation Index)>3, white boxes SI<3.

FIG. 4: The average Stimulation Index (SI) for each peptide, as measured in an IFNγ ELISpot assay, plotted against the predicted TRIA score of the corresponding peptide. Abu-SLP27 is indicated (φ).

The invention is further explained in the following examples. These examples do not limit the scope of the invention, but merely serve to clarify the invention.

EXAMPLES Introduction

In the current invention, we developed an optimal T cell inducing vaccine composition consisting of synthetic long peptides to treat chronically HBV-infected patients. A selection of 37 long peptides (Table 3; sequences ranging from 30 to 39 amino acids) was made encompassing the regions of the HBV Polymerase, Core protein, Surface Antigen and X-protein with the highest putative T cell immunity inducing capacity. To this end first putative HLA class I restricted cytotoxic T cell (CTL) epitopes and putative HLA class II restricted T helper epitopes were identified in these proteins using algorithms that predict HLA class I and II peptide binding and C-terminal generation by the proteasome of all HLA class I binding short peptides (with a length of a CTL epitope; 8-12 aa) contained in the HBV proteins. Numerical values were assigned to all putative CTL epitopes and T helper epitopes reflecting their immunogenicity quality. The quality of any CTL epitope was assessed using the so-called Class I-BCI score (Class I-Binding-Cleavage-Immunogenicity score), incorporating the combination of the HLA class I binding capacity of the epitope in conjunction with the likelihood of its C-terminal liberation from the source protein by the proteasome. Putative T helper epitopes were assessed using the so-called Class II-B score (Class II-Binding score) reflecting their binding capacity and thus predicted immunogenic quality. The combined cumulative value, i.e. the sum of the cumulative Class I-BCI score and the cumulative Class II-B score, was calculated for all possible long peptides, reflecting the cumulative quantity and quality of all CTL epitopes and T helper epitopes, and is expressed in the T cell Regional Immunogenicity Assessment (TRIA) score. Accordingly, the TRIA score enabled the assessment of the total T cell immunogenicity of any possible long peptide (length 30-39 aa) in the HBV proteins. The 37 HBV-derived long peptides with the highest TRIA scores were selected.

Next, we assessed whether naïve donors and donors that have cleared an HBV infection in the past are able to respond to one or more of a subset of 13 long peptides with varying TRIA scores selected from the broad set of 37 long peptides.

PBMC were obtained from buffy coats of twelve healthy donors, six of which were HBV-naïve and six others had cleared an HBV-infection in the past. Using long-term T cell induction assays, we found responses against 12 out of 13 peptides in naïve donors (eleven of which induced responses in multiple donors), confirming the ability of these SLPs to induce T cell responses in a great majority of individuals that had not encountered the antigens before. The strength of T cell responses found in PBMC of HBV-immune donors against these 13 long vaccine peptides correlated with their predicted strength of overall T cell immunogenicity, as expressed in their TRIA scores, validating the predictive value of the TRIA score for selecting immunogenic peptides. Thus the TRIA score is a reliable criterion for the selection of optimal immunogenic long peptides, invigorating us to select the long peptides with the highest TRIA scores into our HBV SLP-based vaccine.

Material and Methods Peptide Synthesis

Peptides were synthesized using solid phase Fmoc/tBu chemistry on a PTI Prelude peptide synthesizer and purified on a Gilson preparative HPLC system to >95% purity. The identity and purity of the peptides were confirmed with UPLC-MS on a Waters Acquity UPLC/TQD system.

Prediction of CTL and T Helper Cell Immunity Inducing Capacity in Selected HBV-Derived SLPs by Net-Based Algorithm

The putative CTL immunity inducing capacity per SLP was predicted by calculating the cumulative Class I-BCI score per SLP. As detailed below, the cumulative BCI score is based on the Class I-B score, which is a measure for HLA class I peptide binding, and the C-score, which is a measure for proteosomal epitope liberation.

The putative T helper cell immunity inducing capacity per SLP was predicted by calculating the cumulative Class II-B score per SLP. As detailed below, the cumulative Class II-B score is based on the Class II-B score, which is a measure for HLA class II peptide binding.

The total putative immunity inducing capacity per SLP was predicted by summation of the cumulative Class I-BCI score and the cumulative Class II-B score, which value is denominated herein as the TRIA score.

Class I-B Score

Peptide binding to 50 HLA class I molecules (see text) of HBV polymerase-derived peptides, HBV Core protein-derived peptides, HBV Surface Antigen-derived peptides and HBV X protein-derived peptides was assessed in silico using a proprietary algorithm. The upper 1.5^(th) percentile of the predicted binding peptides to each HLA class I molecule was selected. The ‘Class I-Binding score (Class I-B score)’ is derived from the ranking of the predicted binding affinity of the peptides. Briefly, the ranking was first reversed and subsequently normalized to 100, so that the peptide predicted to bind best has a score of 100. Example: five peptides were selected (5 within the 1.5^(th) percentile). Peptides were first assigned the ‘reverse ranking score’ 5 to 1 (5 for the best binding peptide). Subsequently, each reverse ranking score is normalized to the number of peptides within the upper 1.5^(th) percentile, so that the best binder scores 100. To that end, the ranking score for each peptide is multiplied with 100/5 (=20). The best binder then obtains a Class I-B score: 5×20=100, the second best binder has a Class I-B score of 4×20=80, etc. In general, the ranking score is multiplied with 100/n (n=number of peptide within the 1.5^(th) percentile). As a consequence, the best predicted binder (to a certain HLA class I molecule) always scores 100, irrespective of the precise number of peptides within the 1.5^(th) percentile that are selected.

C-Score

C-terminal generation by the proteasome of the upper 1.5^(th) percentile of predicted high affinity binding peptides of HBV polymerase, HBV Core protein, HBV Surface Antigen and HBV X-protein (for each HLA class I molecule) was assessed using two proprietary algorithms, which predict the likelihood of a proteasomal cleavage after a certain amino acid position in HBV polymerase, HBV Core protein, HBV Surface Antigen and HBV X-protein, respectively, and can score between 0 and 1, where a higher value represents a higher likelihood of cleavage after the amino acid. The value 0.5 may be used as an arbitrary threshold value: >0.5 the cleavage is likely to occur, and <0.5 the cleavage is likely to not occur. Accordingly, a value close to 1 indicates a high likelihood of cleavage after the specific residue. Because great differences between the predictions by both different algorithms occur, we developed the Cleavage score (C-score) that takes into account the prediction results of both proprietary algorithms. The C-score is the summation of the separate scores by both methods. Therefore, the C-score for each position in HBV polymerase is maximally (close to) 2, and minimally (close to) 0, where close to 2 reflects a very high likelihood by BOTH methods that the cleavage after the residue will be produced by the proteasome, and a C-score close to 1 is considered as an indifferent tendency for cleavage by the proteasome (as predicted on average by both network methods).

Class I-BCI Score

To incorporate in one quantitative measure both the Class I-B score and the C-score, which are the measures indicative for the likelihood that a peptide will bind with high affinity to HLA class I molecules and will be C-terminally produced, the Class I-Binding-Cleavage-Immunogenicity (Class I-BCI) score was developed. The Class I-BCI score is the Class I-B score multiplied by the C-score. As such the Class I-BCI can attain a maximal value of 200 (100×2) (arbitrary units).

Cumulative Class I-BCI Score

The cumulative Class I-BCI score for each long peptide according to the invention was used as (one of two) selection criterion to identify the peptides of the invention. The cumulative Class I-BCI score is a quantitative reflection of both the total number of CD8⁺ cytotoxic T cell epitopes that are contained in a long peptide according to the invention and their predicted quality, in terms of binding capacity and likelihood of intracellular generation by the proteasome, and is as such indicative for the CD8⁺ cytotoxic T cell-inducing power of each peptide according to the invention (its CD8⁺ T cell immunogenicity). A relatively high cumulative Class I-BCI score of a peptide according to the invention indicates a high CD8⁺ T cell immunogenicity.

Class II-B Score

Peptide binding to 13 prevalent HLA class II molecules of HBV polymerase-derived peptides, HBV Core protein-derived peptides, HBV Surface Antigen-derived peptides and HBV X protein-derived peptides was assessed in silico using a proprietary algorithm. The ‘Class II-Binding score’ (Class II-B score) is derived from the ranking of the predicted binding affinity of the peptides. Briefly, the ranking was first reversed and subsequently normalized to 100, so that the peptide predicted to bind best has a score of 100. To reduce the number of peptides in the list, all length variants of peptides predicted to bind to a particular HLA class II molecule with a lower predicted binding (lower Class II-B score) are discarded in the list.

Cumulative Class II-B Score

The cumulative Class II-B score for each long peptide according to the invention was used as the second selection criterion to identify the peptides of the invention. The cumulative Class II-B score is a quantitative reflection of both the total number of CD4⁺ T-helper cell epitopes that are contained in a long peptide according to the invention and their predicted quality, in terms of binding capacity, and is as such indicative for the CD4⁺ T cell-inducing power of each peptide according to the invention (its CD4⁺ T cell immunogenicity). A relatively high cumulative Class II-B score of a peptide according to the invention indicates a high CD4⁺ T cell immunogenicity

T Cell Regional Immunogenicity Assessment (TRIA) Score

The TRIA score for a particular peptide of the invention (SLP) is the sum of cumulative Class I-BCI score and the cumulative Class II-B score of that particular long peptide of the invention (SLP).

Proteasomal Digestion

Dithiotreitol (DTT; Sigma-Aldrich) was freshly dissolved in UPLC-grade water and added to a 2× concentrated proteasome digestion buffer (60 mM Trizma-base; pH 7.5; Sigma-Aldrich, 20 mM KCl; Sigma-Aldrich, 10 mM MgCl₂; Sigma-Aldrich, 10 mM NaCl; Sigma-Aldrich) to an end concentration DTT of 2 mM. Then, 130 μl UPLC-grade water was added to 3 reaction vials, along with 150 μl of the 2× concentrated proteasome digestion buffer containing 2 mM DTT, and 10 μl of the peptide to be tested (stock concentration 300 nmol/ml). After vortexing the vials, 10 μl of water was added to vial 1 (mock control digest), 1 μg (10 μl) of constitutive 20S-proteasome (stock 0.1 mg/ml; Enzo Life Sciences) to vial 2, and 1 μg (10 μl) of immune 20S-proteasome (stock 0.1 mg/ml; Enzo Life Sciences) to vial 3. A 50 μl sample for T=0 was taken directly after vortexing and 4 μl of Formic acid (Sigma-Aldrich) was added to stop the reaction. The reaction vials were vortexed and incubated at 37° C. Samples of 50 μl were collected after 1 h, 3 h, 6 h and 24 h incubation. The reactions were stopped with 4 μl Formic acid, and all samples were stored at 20° C.

Mass Spectrometry Analysis of Digested Fragments

A Q-TOF1 mass spectrometer (Waters) equipped with an online nanoelectrospray interface with an approximate flow rate of 250 nl/min was used for electrospray ionization-mass spectrometry. Peptide-digestion samples were trapped on a precolumn (MCA-300-05-C18; Dionex) and were eluted with a steep gradient of 70-90% buffer B over 10 min (buffer A, water, acetonitrile and formic acid, 95:3:1 (vol/vol/vol); buffer B, water, acetonitrile and formic acid, 10:90:1 (vol/vol/vol)). Mass spectra were recorded from a mass of 50-2000 daltons. In tandem mass spectrometry mode, ions were selected with a window of 3 daltons. The collision gas was argon (4×10⁻⁵ mbar), and the collision voltage was ˜30 V. For peptide digestion by purified constitutive proteasome and immunoproteasome, peaks in the mass spectra were searched in source substrate peptides with BioLynx software (Waters) and the abundance of a specific digestion fragment was assessed quantitatively as its percentage of the total summed intensities, including undigested substrate.

Cells

Peripheral blood mononuclear cells (PBMC) from healthy donors were isolated by centrifugation over a Ficoll gradient. To generate dendritic cells (DCs), approximately 50*10⁶ PBMC were brought to a concentration of 3*10⁶ cells/ml complete medium (IMDM, Lonza, supplemented with 8% HS, Seralab; penicillin/streptomycin, Lonza; L-glutamin, Lonza) and seeded 3 ml/well in a 6-wells plate (Corning). After incubation for 1.5 hours at 37° C., non-adherent cells were washed away in three washing steps using complete medium (day 0). The adherent cells were cultured for three days at 37° C. in 2 ml/well of complete medium containing 800 U/ml GM-CSF and 500 U/ml IL-4 (Peprotech). On day 3, 1 ml of complete medium containing 2400 U/ml GM-C SF and 1500 U/ml IL-4 was added to each well and cultured for another three days at 37° C.

Induction of T Cells

On day 6, long peptides distributed over 3 pools were added to monocyte-derived DCs of naïve donors at a 3 nmol/ml concentration and incubated overnight at 37° C. Pool 1 comprises SLP 26 (SEQ ID NO: 76), SLP 24 (SEQ ID NO: 74), SLP 1 (SEQ ID NO: 51) and SLP 30 (SEQ ID NO: 1142); Pool 2 comprises Abu-SLP 27 (SEQ ID NO: 77, wherein the cysteine on amino acid position 1 is replaced by Abu), SLP 25 (SEQ ID NO: 75), SLP 10 (SEQ ID NO: 60) and SLP 34 (SEQ ID NO: 1469); and Pool 3 comprises SLP 5 (SEQ ID NO: 55), SLP 13 (SEQ ID NO: 63), SLP 14 (SEQ ID NO: 64) and SLP 21 (SEQ ID NO: 21). On day 7, the cells were washed twice with complete medium to remove peptides. DC and autologous PBMC were co-cultured in a 1:10 ratio for 10 days at 37° C. in the presence of 10 ng/ml IL-7 and 100 pg/ml IL-12p70. The T cell lines generated by this process were checked every 2-3 days and split when necessary.

Restimulation of T Cell Lines

Three days after T cell induction (day 10), a second batch of autologous DC was differentiated and loaded with peptide pools as described above. On day 10 after initiation of the T cell line (day 17), the peptide-loaded DC were washed twice with complete medium and added to the T cells in a 1:10 (DC:T cell) ratio in the presence of 10 ng/ml IL-7 and 100 pg/ml IL-12p70. The cells were co-cultured for 7 days. On day 17, also a new batch of DC was differentiated and loaded with peptide pools as described above. For this second restimulation, starting on day 24, DC and T cells were co-cultured in a 1:10 ratio. Two days after restimulation, 30 IU/ml IL-2 (Peprotech) and 5 ng/ml IL-15 (Peprotech) were added to the culture medium. A third restimulation, starting on day 31, was performed identically to the second restimulation.

T Cell Proliferation and IFNγ Production

To measure T cell activation and proliferation, autologous DC were loaded for 6 hours with each of the 13 HBV-derived peptides separately on day 23, 30 and 37 of the T cell induction protocol described above. The DCs were washed and 5,000 peptide-loaded DC were co-cultured with 50,000 T cells for 48 hours. Then, supernatant was collected for ELISA (IFNγ ELISA, Diaclone) and culture medium containing ³H thymidine was added to all wells. Radioactive ³H thymidine is incorporated in the DNA of newly formed (proliferated) cells, which is measured after 16 hours of incubation on a MicroBeta liquid scintillation counter (Wallac/Perkin Elmer).

IFNγ-ELISpot

To detect antigen-specific IFNγ-producing human T cells, the PBMC were first pre-stimulated with 3 nmol/ml of the indicated peptide for 72 hours at 37° C. During this stimulation, ELISpot PVDF plates (Mabtech) were coated with 5 ug/ml anti-human IFNγ mAb 1-D1K coating antibody (Mabtech) in PBS and incubated overnight at 4° C. After stimulation of the PBMC, the coating antibody was aspirated from the plate, and washed 4 times with PBS. To block aspecific binding, 100 μl of IMDM containing 8% FCS was added to all wells and incubated at 37° C. for 1 hour. In the meantime, stimulated PBMC were harvested, centrifuged, resuspended in X-vivo 15 medium (Lonza) and counted. All PBMC samples were brought to a concentration of 1.5*10⁶ cells/ml in X-vivo 15 medium. The medium in the wells of the PVDF plate was aspirated and 100 μl of each PBMC sample was added to the plate in quadruplicates. The plates were incubated at 37° C. overnight. The next day, the supernatant was discarded and plates are washed 6 times with PBS/Tween20 0.05%. The biotinylated anti-human IFNγ mAb 7-B6-1 (Mabtech) was added to all wells (100 μl/well) at a 0.3 μg/ml concentration in PBS with 1% FBS, and incubated for 2 hours at RT. Next, plates were washed 6 times using PBS/Tween20 0.05% and 1 μg/ml Extravidin-Alkaline phosphatase (ALP) (Sigma-Aldrich) was added to all wells (100 μl/well) in PBS with 1% FBS. The plates were incubated for 1 hour at RT. ALP substrate solution BCIP/NBT-plus (Mabtech) was prepared and 100 μl/well was added to all wells after the plates were washed 4 times with PBS/Tween20 0.05%. To terminate the colorimetric reaction (after 1-20 minutes), tap water was used to wash the plates extensively. After drying, the formed spots were measured on a Biosys Bioreader 5000.

Results Selection of Long Peptides Based on HLA Class I Peptide Binding Prediction and Predicted C-Terminal Generation of all Possible CD8⁺ T Cell Epitopes Contained in the Long Peptides

A high quality CD8⁺ T cell epitope is defined as a peptide that possesses both a predicted high affinity for the HLA class I molecule to which it binds and is also predicted to be generated at its C-terminus by a proteolytic cleavage of the proteasome. Peptides according to the present invention were selected in HBV protein regions that contain optimally high numbers of high quality CD8⁺ and CD4⁺ T cell epitopes. To this end, first the HLA class I binding and C-terminal generation of all possible CD8⁺ T cell epitopes was assessed using a proprietary HLA class I peptide binding algorithm and two proprietary algorithms predicting the cleavages by the proteasome. Subsequently, we devised a single quantitative measure, the so-called binding-cleavage-immunogenicity (BCI) Class I-score, that for each short peptide (8-13 amino acids) incorporates both its predicted binding affinity for the HLA class I molecule to which it binds and the likelihood that the peptide is generated by the proteasome in the cells. The Class I-BCI score is calculated from (1) the binding Class I-score (Class I-B score), which is derived from the results of the in silico prediction of HLA class I peptide binding using the aforementioned algorithm, and (2) the cleavage score (C-score), which is derived from the results of the in silico prediction of the proteasome-mediated C-terminal generation of the peptide by the proteasome using the aforementioned algorithms. Tables 4a, 5a, 6a, and 7a present the Class I-BCI score for all possible CD8⁺ T cell epitopes of these Polymerase, Core protein, Surface Antigen or X-protein derived SLPs, respectively, together with the cumulative BCI Class I score. Tables 4b, 5b, 6b and 7b present the Class II-B score for all possible CD4⁺ T cell epitopes of these Polymerase, Core protein, Surface Antigen or X-protein derived SLPs, respectively, together with the cumulative Class II-B score. Together the cumulative Class I-BCI score (for CTL epitopes) and the cumulative B Class II-score (for T helper epitopes) resulted in one quantitative value, the so-called Total Regional Immunogenicity Assessment (TRIA) score, reflecting the overall T cell immunogenicity of a long vaccine peptide (Table 3). Based on the highest TRIA scores, 37 SLPs derived from HBV Polymerase, Core protein, Surface Antigen or X-protein were selected for further evaluation (Table 3). From these, to validate the predictive power of the TRIA score, we chose a representative set of 13 SLPs, which included SLP with relatively low and high TRIA scores, for in vitro immunogenicity assessment. These 13 peptides were divided over three peptide pools for T cell induction assays, as described (see below).

Peptide Fragment Analysis after Proteasomal Digestion of SLPs Reveals High Accuracy of in Silico Predictions

An important component of the identification of putative CTL epitopes is the prediction of their C-terminal generation by a proteasome-mediated cleavage. To validate the reliability of this prediction, proteasomal digestion patterns were experimentally assessed for all but 3 of the 13 functionally tested long vaccine peptides (three long peptides were not being cleaved due to technical reasons).

Digestion experiments were performed separately with 20S constitutive proteasomes and 20S immuno proteasome preparations. The combined analysis of cleavages produced by both types of proteasomes allows the assessment of the C-terminal generation of CTL epitopes that are expressed both on the surface of antigen presenting cells (mainly dendritic cells), containing immunoproteasomes, and on the surface of cancer cells, especially from solid tumors, which mainly express constitutive proteasomes. For vaccination purposes these epitopes are preferred because vaccination with such epitopes will allow the induction of CTL by vaccination and the subsequent eradication of cancer cells by these CTL after recognition of the epitopes on the surface of cancer cells.

As indicated in FIG. 1, 10 long peptides of the invention (length 30-39 aa) were co-incubated in an appropriate buffer with the proteasome preparations at 37° C. for 0, 1, 3, 6 and 24 h. After incubation for the indicated interval reactions were stopped and digestion mixtures, containing the digestion fragments, were measured by mass spectrometry as described herein. The mass spectra were (semi-quantitatively) analyzed to assess the position and abundance of the cleavage sites. The results of 24 h digestion are shown in FIG. 1.

The observed cleavage sites observed after 24 h incubation are indicated with arrows. Only cleavage sites that were observed in both the digestion with constitutive proteasomes and the digestion with immunoproteasomes are shown. Major cleavage sites and minor cleavages sites at 24 h digestion are depicted with bold and thin arrows, respectively, according to the following classification:

Major cleavage site: fragments containing as COOH terminus the residue NH₂-terminal from the cleavage site together with the (possible) complementary fragment(s) are present for ≥7% at 24 h incubation, as calculated from the intensities of the fragment peaks in the mass spectra. Minor cleavage site: fragments containing as COOH terminus the residue NH₂-terminal from the cleavage site together with the (possible) complementary fragment(s) are present for <7% at 24 h incubation. Cleavage sites with a cumulative fragment abundance of <1% are not shown.

FIG. 1 also indicates the C-score of proteasomal cleavage prediction. This score indicates the likelihood of cleavage C-terminal of the residue directly under the C-score. If the C-score>1 the cleavage site is considered predicted to be cleaved by both the constitutive proteasome and the immunoproteasome. As described herein, the C-score is a summation of the predictions by two in silico algorithms separately predicting the proteasome-mediated cleavages by constitutive proteasomes and the cleavages by immunoproteasomes. Each separate prediction can attain a maximal value of 1. Accordingly, the maximal value of the C-score is 2. C-scores>1 are together counted as the total number of predicted cleavage sites (the C-terminus of the long substrate peptide is not taken into account, because cleavage after this residue cannot be tested).

FIG. 1 further indicates the confirmed cleavages (indicated by ‘+’), which are those predicted cleavage sites (C-score>1) that are confirmed to be cleaved after 24 h in the proteasome-mediated digestion assay.

As indicated by FIG. 1, for SLP1 36% (4/11), for SLP10 71% (10/14), for SLP13 62% (10/16), for SLP14 100% (13/13), for SLP18 65% (13/20), for SLP21 87% (14/16), for SLP24 62% (10/16), for SLP25 57% (8/14), for SLP26 72% (8/11), and for SLP27 75% (9/12) of the predicted cleavage sites have been confirmed here.

Induction of T Cell Responses Against 12 Out of 13 Selected Peptides in a Naïve Population

To assess whether the 13 selected peptides are able to induce a T cell response in naïve donors, PBMC were isolated from buffy coats derived from six healthy donors that had not experienced an HBV-infection. These PBMC were restimulated with either of the 3 peptide pools to obtain T cell lines, that were subsequently stimulated with the selected 13 peptides. The production of IFNγ and T cell proliferation (³H thymidine incorporation) were measured as a read-out for T cell activation. Results are shown in FIG. 2, indicating the percentage of donors showing a positive T cell response with a stimulation index (SI) of 1.5 or higher. The SI is calculated by dividing the measured sample value by the value of non-stimulated control cells. Induced responses in naïve donors were detected against 12 of the 13 pre-selected peptides, while 11 pre-selected peptides induced a response in multiple naïve donors.

Strength of Pre-Existing T Cell Responses in HBV-Immune Donors Correlates with TRIA Score

Subjects that have gone through an HBV infection and successfully cleared it, possess circulating memory T cells specific for HBV. To assess the relevance of the selected vaccine peptides for the clearance of a naturally occurring HBV infection, we tested the presence of T cell responses against the 13 selected HBV peptides in PBMC derived from six HBV-immune donors. After isolation of the PBMC, cells were stimulated with each of the 13 peptides and an IFNγ-ELISpot was performed to detect T cell responses. PBMC samples from 3 out of 6 tested donors showed a positive IFNγ response against one or more of the 13 peptides (SI>3). Responses were observed against 11 (SLP 5, 10, 13, 14, 18, 21, 24, 25, 26, 27 and 34, represented by SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 76, 77 and 1469, respectively) out of the 13 peptides, 6 of which induced responses in multiple donors (SLP 10, 13, 21, 24, 25 and 34, represented by SEQ ID NO: 60, 63, 71, 74, 75 and 1469, respectively). The results are summarized in FIG. 3, indicating the donors showing a positive IFNγ⁺ T cell response against a peptide. For each SLP tested, the average SI of the IFNγ-responses was calculated; 1.21 for SLP1, 2.11 for SLP5, 2.40 for SLP10, 2.44 for SLP13, 1.97 for SLP14, 1.86 for SLP18, 2.87 for SLP21, 2.54 for SLP24, 2.66 for SLP25, 1.56 for SLP26, 1.66 for Abu-SLP27, 1.49 for SLP30 and 3.02 for SLP34. Importantly, when the average SI of the IFNγ-responses to each peptide is plotted against the corresponding TRIA score, we see a significant correlation (FIG. 4), both while including (R²=0.37, p=0.028; see FIG. 4) the results of Abu-SLP27 and while excluding (R²=0.34, p=0.048; not shown) the results of Abu-SLP27. This validates the use of the TRIA score for the selection of immunogenic peptides.

Discussion

The experimental results presented herein validate, and therefore support, the selection and underscore the immunological relevance of the HBV-derived long vaccine peptides of the present invention. These long vaccine peptides encompass the HBV protein regions with the highest number of high quality HLA class I and HLA class II binding epitopes in an outbred population. A preferred combination of the vaccine peptides will be incorporated in a novel HBV SLP vaccine composition to treat chronically HBV-infected patients. Using algorithms to predict the peptide binding affinity of short peptides (8-12 aa) for all prevalent HLA class I molecules and the likelihood of the C-terminal generation of these short peptides by cleavage by the proteasome, in combination with the identification of the putative T helper epitopes, we identified highly immunogenic regions from which the optimal 37 long vaccine peptides were selected.

To enable proper selection of long vaccine peptides in the present invention, a quantitative measure was developed, the TRIA score. Without such a quantitative measure attributed to all possible long HBV peptides, a proper selection of the optimal long peptides is not possible. The TRIA score is a quantitative representation of the quality and quantity of all putative HLA class I restricted CD8⁺ cytotoxic T cell epitopes and HLA class II restricted CD4⁺ T helper epitopes contained in a long peptide. The TRIA score was calculated for all possible HBV peptides with a length of 30-39 aa, which is the optimal peptide length for vaccination purposes, enabling the rational selection of a set of highly immunogenic long vaccine peptides.

For further testing and validation of the immunological relevance, we selected a set of 13 SLP with varying TRIA scores. First, we experimentally digested these SLP using either constitutive proteasome or immunoproteasome. The generated fragments showed a clear overlap with the predicted C-terminal cleavage sites, expressed in the BCI score.

Thereafter, T cell assays were performed using PBMC from both naïve and HBV-immune donors. Nearly all 13 selected SLPs were able to induce T cell responses in PBMC derived from naïve healthy donors, which proves that the selected SLP set has the potential to induce responses by the T cell repertoire that had not been stimulated before. Within the same set of vaccine peptides, a strong correlation was observed between the TRIA score of a certain vaccine peptide and the strength of the IFNγ-response in HBV-immune donors, indicating that the TRIA score is a predictive value for in vivo immunogenicity and thus functionality of the vaccine peptides.

TABLE 1 Protein and DNA sequences of HBV polymerase, HBV core and HBV large surface proteins. SEQ ID Gene / Gene NO: SEQ type product Sequence 1 Protein HBV MPLSYQHFRKLLLLDDGTEAGPLEEELPRLADADLHRRVAE Polymerase DLNLGNLNVSIPWTHKVGNFTGLYSSTVPIFNPEWQTPSFP KIHLQEDIINRCQQFVGPLTVNEKRRLKLIMPARFYPTHTK YLPLDKGIKPYYPDQVVNHYFQTRHYLHTLWKAGILYKRET TRSASFCGSPYSWEQELQHGRLVIKTSQRHGDESFCSQSSG ILSRSSVGPCIRSQLKQSRLGLQPRQGRLASSQPSRSGSIR AKAHPSTRRYFGVEPSGSGHIDHSVNNSSSCLHQSAVRKAA YSHLSTSKRQSSSGHAVEFHCLPPNSAGSQSQGSVSSCWWL QFRNSKPCSEYCLSHLVNLREDWGPCDEHGEHHIRIPRTPA RVTGGVFLVDKNPHNTAESRLVVDFSQFSRGISRVSWPKFA VPNLQSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLI GSSGLSRYVARLSSNSRINNNQYGTMQNLHDSCSRQLYVSL MLLYKTYGWKLHLYSHPIVLGFRKIPMGVGLSPFLLAQFTS AICSVVRRAFPHCLAFSYMDDVVLGAKSVQHRESLYTAVTN FLLSLGTHLNPNKTKRWGYSLNFMGYIIGSWGTLPQDHIVQ KIKHCFRKLPVNRPIDWKVCQRIVGLLGFAAPFTQCGYPAL MPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVARQRPGLC QVFADATPTGWGLAIGHQRMRGTFVAPLPIHTAELLAACFA RSRSGAKLIGTDNSVVLSRKYTSFPWLLGCTANWILRGTSF VYVPSALNPADDPSRGRLGLSRPLLRLPFQPTTGRTSLYAV SPSVPSHLPVRVHFASPLHVAWRPP 2 CDS HBV See sequence listing Polymerase 3 Genomic HBV genome See sequence listing 4 Protein HBV Core MQLFHLCLIISCTCPTVQASKLCLGWLWGMDIDPYKEFGAT VELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHT ALRQAILCWGELMTLATWVGNNLEDPASRDLVVNYVNTNVG LKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPP NAPILSTLPETTVVRRRDRGRSPRRRTPSPRRRRSPSPRRR RSQSRESQC 5 CDS HBV Core See sequence listing 1141 Protein HBV MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNP large surface DWDFNPVKDDWPAANQVGVGAFGPRLTPPHGGILGWSPQAQ protein GILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWN STAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSI SARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQS LDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGY RWMCLRRFITFLFILLLCLIFLLVLLDYQGMLPVCPLIPGS TTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPS SWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAI WMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI

TABLE 2 Different HBV X protein variants and the deduced consensus protein sequence. Number of mismatches as compared SEQ ID UniProt to consensus NO. ENTRY HBV genotype source sequence X protein sequence 6 Q91C38 Hepatitis B virus genotype A1 subtype adw2 12 see sequence listing (isolate South Africa/84/2001)(HBV-A) 7 O91531 Hepatitis B virus genotype A2 9 see sequence listing (isolate Japan/11D11HCCW/1998)(HBV-A) 8 P69714 Hepatitis B virus genotype A2 subtype adw 8 see sequence listing (isolate Japan/Nishioka/1983)(HBV-A) 9 P17102 Hepatitis B virus genotype A2 subtype adw2 7 see sequence listing (isolate Germany/991/1990)(HBV-A) 10 P69713 Hepatitis B virus genotype A2 subtype adw2 7 see sequence listing (strain Rutter 1979)(HBV-A) 11 Q4R1S1 Hepatitis B virus genotype A3 16 see sequence listing (isolate Cameroon/CMR711/1994)(HBV-A) 12 Q4R1S9 Hepatitis B virus genotype A3 15 see sequence listing (isolate Cameroon/CMR983/1994)(HBV-A) 13 P0C678 Hepatitis B virus genotype B1 II see sequence listing (isolate Japan/Ry30/2002)(HBV-B) 14 Q9PX75 Hepatitis B virus genotype B1 12 see sequence listing (isolate Japan/Yamagata-2/1998)(HBV-B) 15 P20976 Hepatitis B virus genotype B1 subtype adw 8 see sequence listing (isolate Japan/pJDW233/1988)(HBV-B) 16 P20975 Hepatitis B virus genotype B2 10 see sequence listing (isolate Indonesia/pIDW420/1988)(HBV-B) 17 Q9PXA2 Hepatitis B virus genotype B2 15 see sequence listing (isolate Vietnam/16091/1992)(HBV-B) 18 P0C685 Hepatitis B virus genotype B2 11 see sequence listing (isolate Vietnam/9873/1997)(HBV-B) 19 Q67923 Hepatitis B virus genotype B2 subtype adw 11 see sequence listing (isolate China/patient4/1996)(HBV-B) 20 P20977 Hepatitis B virus genotype B/C subtype adw 12 see sequence listing (isolate Okinawa/pODW282/1998)(HBV-B) 21 Q9E6S8 Hepatitis B virus genotype C 6 see sequence listing (isolate Vietnam/3270/2000)(HBV-C) 22 P0C686 Hepatitis B virus genotype C subtype adr 9 see sequence listing (isolate Japan/Nishioka/1983)(HBV-C) 23 P12936 Hepatitis B virus genotype C subtype adr 8 see sequence listing (strain Japan/adr4/1983)(HBV-C) 24 Q9YZR6 Hepatitis B virus genotype C subtype ar 10 see sequence listing (isolate Japan/S-207/1988)(HBV-C) 25 Q69027 Hepatitis B virus genotype C subtype ayr 8 see sequence listing (isolate Human/Japan/Okamoto/-)(HBV-C) 26 P0C687 Hepatitis B virus genotype C subtype ayw 14 see sequence listing (isolate Australia/AustRC/1992)(HBV-C) 27 Q913A9 Hepatitis B virus genotype C subtype ayw 5 see sequence listing (isolate China/Tibet127/2002)(HBV-C) 28 P24026 Hepatitis B virus genotype D 12 see sequence listing (isolate France/alpha1/1989)(HBV-D) 29 O93195 Hepatitis B virus genotype D 14 see sequence listing (isolate Germany/1-91/1991)(HBV-D) 30 P0C681 Hepatitis B virus genotype D subtype ayw 9 see sequence listing (isolate Australia/AustKW/1991)(HBV-D) 31 P03165 Hepatitis B virus genotype D subtype ayw 7 see sequence listing (isolate France/Tiollais/1979)(HBV-D) 32 Q67877 Hepatitis B virus genotype D subtype ayw 8 see sequence listing (isolate Italy/C1/1992)(HBV-D) 33 Q9QMI3 Hepatitis B virus genotype D subtype ayw 9 see sequence listing (isolate Japan/JYW796/1988)(HBV-D) 34 Q80IU8 Hepatitis B virus genotype E 11 see sequence listing (isolate Cote d'Ivoire/ABI-129/2003)(HBV-E) 35 Q80IU5 Hepatitis B virus genotype E 7 see sequence listing (isolate Cote d'Ivoire/ABI-212/2003)(HBV-E) 36 Q69604 Hepatitis B virus genotype E subtype ayw4 8 see sequence listing (isolate Kou)(HBV-E) 37 Q8JMY3 Hepatitis B virus genotype F1 subtype adw4 20 see sequence listing (isolate El Salvador/1116Sal/1997)(HBV-F) 38 Q99HR6 Hepatitis B virus genotype F2 19 see sequence listing (isolate Argentina/sal6/2000)(HBV-F) 39 Q05499 Hepatitis B virus genotype F2 21 see sequence listing (isolate Brazil/w4B)(HBV-F) 40 Q69607 Hepatitis B virus genotype F2 subtype adw4q 21 see sequence listing (isolate Senegal/9203)(HBV-F) 41 Q9IBI5 Hepatitis B virus genotype G 31 see sequence listing (isolate IG29227/2000)(HBV-G) 42 Q8JMY5 Hepatitis B virus genotype H 22 see sequence listing (isolate United States/LAS2523/2002)(HBV-H) 43 Q8JN06 Hepatitis B virus genotype H subtype adw4 22 see sequence listing (isolate Nicaragua/1853Nic/1997)(HBV-H) 44 Q8JMZ5 Hepatitis B virus genotype H subtype adw4 22 see sequence listing (isolate Nicaragua/2928Nic/1997)(HBV-H) 45 — Consensus aa sequence — MAARLCCQLDPARDVLCLRPV GAESRGRPLSGPLGALPSPSP SAVPADHGAHLSLRGLPVCAF SSAGPCALRFTSARRMETTVN AHQILPKVLHKRTLGLSAMST TDLEAYFKDCVFKDWEELGEE IRLKVFVLGGCRHKLVCSPAP CNFFTSA

TABLE 3 Synthetic long peptide (SLP) sequences. Cumula- Cumula- tive SEQ tive Class ID Class  II-B TRIA NO: SLP# I-BCI^(A) score^(B) score^(C) Source Sequence 51 SLP1 7264 780 8044 HBV Polymerase aa 1 - 30 MPLSYQHFRKLLLLDDGTEAGPLEEELPRL 52 SLP2 6943 1323 8266 HBV Polymerase aa 52 - 86 IPWTHKVGNFTGLYSSTVPIFNPEWQTPSFPKIHL 53 SLP3 6469 3070 9539 HBV Polymerase aa 103 - 135 VNEKRRLKLIMPARFYPTHTKYLPLDKGIKPYY 54 SLP4 6169 143 6312 HBV Polymerase aa 118 - 150 YPTHTKYLPLDKGIKPYYPDQVVNHYFQTRHYL 55 SLP5 11815 1519 13334 HBV Polymerase aa 139 - 177 VVNHYFQTRHYLHTLWKAGILYKRETTRSASFCGSPYSW 56 SLP6 10432 928 11360 HBV Polymerase aa 143 - 177 YFQTRHYLHTLWKAGILYKRETTRSASFCGSPYSW 57 SLP7 10325 1817 12142 HBV Polymerase aa 137- 170 DQVVNHYFQTRHYLHTLWKAGILYKRETTRSASF 58 SLP8 7246 3 7249 HBV Polymerase aa 316 - 347 SQSQGSVSSCWWLQFRNSKPCSEYCLSHLVNL 59 SLP9 6722 527 7249 HBV Polymerase aa 385 - 417 TAESRLVVDFSQFSRGISRVSWPKFAVPNLQSL 60 SLP10 11926 943 12869 HBV Polymerase aa 419 - 456 NLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLIGSSGL 61 SLP11 12384 1058 13442 HBV Polymerase aa 422 - 459 SSNLSWLSLDVSAAFYHIPLHPAAMPHLLIGSSGLSRY 62 SLP12 12198 426 12624 HBV Polymerase aa 427 - 459 WLSLDVSAAFYHIPLHPAAMPHLLIGSSGLSRY 63 SLP13 15733 3046 18779 HBV Polymerase aa 481 - 514 HDSCSRQLYVSLMLLYKTYGWKLHLYSHPIVLGF 64 SLP14 12015 1042 13057 HBV Polymerase aa 524 - 559 SPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGA 65 SLP15 11658 783 12441 HBV Polymerase aa 526 - 559 FLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGA 66 SLP16 8255 1482 9737 HBV Polymerase aa 565 - 598 RESLYTAVTNFLLSLGIHLNPNKTKRWGYSLNFM 67 SLP17 6396 223 6619 HBV Polymerase aa 584 - 617 NPNKTKRWGYSLNFMGYIIGSWGTLPQDHIVQKI 68 SLP18 12576 1365 13941 HBV Polymerase aa 653 - 691 YPALMPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVAR 69 SLP19 10420 1181 11601 HBV Polymerase aa 657 - 691 MPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVAR 70 SLP20 7869 244 8113 HBV Polymerase aa 715 - 746 QRMRGTFVAPLPIHTAELLAACFARSRSGAKL 71 SLP21 8555 1591 10146 HBV Polymerase aa 754 - 791 VLSRKYTSFPWLLGCTANWILRGTSFVYVPSALNPADD 72 SLP22 6817 1709 8526 HBV Polymerase aa 757 - 792 RKYTSFPWLLGCTANWILRGTSFVYVPSALNPADDP 73 SLP23 8553 903 9456 HBV Polymerase aa 754 - 789 VLSRKYTSFPWLLGCTANWILRGTSFVYVPSALNPA 74 SLP24 7277 4649 11926 HBV Core aa 107 - 141 DPASRDLVVNYVNTNVGLKIRQLLWFHISCLTFGR 75 SLP25 11331 5493 16824 HBV Core aa 136 - 169 CLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPIL 76 SLP26 5422 4414 9836 HBV consensus seq X protein ALPSPSPSAVPADHGAHLSLRGLPVCAFSSAGP aa 36 - 68 77 SLP27 6468 3788 10256 HBV consensus seq X protein CAFSSAGPCALRFTSARRMETTVNAHQILPKVLHK aa 61 - 95 78 SLP28 7354 3170 10524 HBV consensus seq X protein HQILPKVLHKRTLGLSAMSTTDLEAYFKDCVFKDW aa 86 -120 79 SLP29 5862 1024 6886 HBV consensus seq X protein LEAYFKDCVFKDWEELGEEIRLKVFVLGGCRHKL aa 108 - 141 1142 SLP30 6882 4798 11680 HBV large surface protein MENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWW aa 175 - 210 1143 SLP31 10214 7238 17452 HBV large surface protein CPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDY aa 239 - 274 1144 SLP32 14976 1815 16791 HBV large surface protein CIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFV aa 323 - 358 1468 SLP33 13107 1815 14922 HBV large surface protein PSSWAFAKYLWEWASVRFSWLSLLVPFVQWFV aa 327 - 358 1469 SLP34 12851 1815 14666 HBV large surface protein SSWAFAKYLWEWASVRFSWLSLLVPFVQWFV aa 328 -358 1145 SLP35 9736 4425 14161 HBV large surface protein WLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI aa 365 - 400 1470 SLP36 5389 4035 9424 HBV large surface protein MMWYWGPSLYSIVSPFIPLLPIFFCLWVYI aa 371 - 400 1471 SLP37 6880 4160 11040 HBV large surface protein WMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI aa 370 - 400 ^(A) Cumulative Class I-BCI score: See Material and Methods (Examples section). ^(B)Cumulative Class II-B score: See Material and Methods (Examples section). ^(C)TRIA score is the sum of the Cumulative Class I-BCI score and the Cumulative Class II-B score.

TABLE 4a Predicted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences from HBV polymerase protein. HLA class I binding peptides in SLP sequences derived from HBV Polymerase protein SEQ Class Class ID HLA class I I-B I-BCI Peptide of invention (SLP) Start End Length Sequence ^(A) NO:  molecule score^(B) C-score^(C) score^(D) SLP# SLP Start SLP End 1 8 8 MPLSYQHF 80 A*6802 9 1.42 13 1 1 30 1 8 8 MPLSYQHF 80 B*0801 20 1.42 29 1 1 30 1 8 8 MPLSYQHF 80 B*1402 62 1.42 88 1 1 30 1 8 8 MPLSYQHF 80 B*1502 13 1.42 18 1 1 30 1 8 8 MPLSYQHF 80 B*1801 57 1.42 81 1 1 30 1 8 8 MPLSYQHF 80 B*3503 96 1.42 136 1 1 30 1 8 8 MPLSYQHF 80 B*5101 77 1.42 109 1 1 30 1 8 8 MPLSYQHF 80 B*5301 92 1.42 130 1 1 30 1 8 8 MPLSYQHF 80 B*5501 26 1.42 36 1 1 30 1 8 8 MPLSYQHF 80 B*5601 23 1.42 33 1 1 30 1 9 9 MPLSYQHFR 81 A*3101 77 1.83 142 1 1 30 1 9 9 MPLSYQHFR 81 A*3303 77 1.83 142 1 1 30 1 9 9 MPLSYQHFR 81 A*6801 78 1.83 143 1 1 30 1 9 9 MPLSYQHFR 81 B*5101 22 1.83 40 1 1 30 2 9 8 PLSYQHFR 82 A*3101 22 1.83 39 1 1 30 2 9 8 PLSYQHFR 82 A*3303 45 1.83 83 1 1 30 2 9 8 PLSYQHFR 82 A*7401 28 1.83 51 1 1 30 1 10 10 MPLSYQHFRK 83 B*3501 41 1.21 50 1 1 30 3 10 8 LSYQHFRK 84 A*0301 90 1.21 110 1 1 30 3 10 8 LSYQHFRK 84 A*1101 89 1.21 108 1 1 30 3 10 8 LSYQHFRK 84 A*3001 43 1.21 53 1 1 30 3 10 8 LSYQHFRK 84 A*7401 45 1.21 55 1 1 30 1 11 11 MPLSYQHFRKL 85 B*0702 87 1.89 165 1 1 30 1 11 11 MPLSYQHFRKL 85 B*0801 97 1.89 183 1 1 30 1 11 11 MPLSYQHFRKL 85 B*1402 96 1.89 182 1 1 30 1 11 11 MPLSYQHFRKL 85 B*3501 45 1.89 86 1 1 30 1 11 11 MPLSYQHFRKL 85 B*3503 86 1.89 164 1 1 30 1 11 11 MPLSYQHFRKL 85 B*3901 58 1.89 111 1 1 30 1 11 11 MPLSYQHFRKL 85 B*5101 90 1.89 170 1 1 30 1 11 11 MPLSYQHFRKL 85 B*5301 66 1.89 124 1 1 30 1 11 11 MPLSYQHFRKL 85 B*5501 79 1.89 150 1 1 30 1 11 11 MPLSYQHFRKL 85 B*5601 62 1.89 117 1 1 30 3 11 9 LSYQHFRKL 86 B*5201 45 1.89 85 1 1 30 4 11 8 SYQHFRKL 87 A*2301 57 1.89 108 1 1 30 4 11 8 SYQHFRKL 87 A*2402 65 1.89 123 1 1 30 3 12 10 LSYQHFRKLL 88 B*5201 37 1.82 68 1 1 30 4 12 9 SYQHFRKLL 89 A*2402 26 1.82 48 1 1 30 5 12 8 YQHFRKLL 90 B*0801 66 1.82 120 1 1 30 5 12 8 YQHFRKLL 90 B*1402 54 1.82 98 1 1 30 5 12 8 YQHFRKLL 90 B*3901 78 1.82 142 1 1 30 5 12 8 YQHFRKLL 90 B*4801 71 1.82 130 1 1 30 3 13 11 LSYQHFRKLLL 91 B*0801 59 1.71 101 1 1 30 3 13 11 LSYQHFRKLLL 91 B*5201 65 1.71 111 1 1 30 3 13 11 LSYQHFRKLLL 91 B*5701 11 1.71 18 1 1 30 4 13 10 SYQHFRKLLL 92 A*2301 28 1.71 47 1 1 30 4 13 10 SYQHFRKLLL 92 A*2402 33 1.71 57 1 1 30 5 13 9 YQHFRKLLL 93 B*0801 31 1.71 52 1 1 30 5 13 9 YQHFRKLLL 93 B*1402 61 1.71 104 1 1 30 5 13 9 YQHFRKLLL 93 B*3901 64 1.71 109 1 1 30 5 13 9 YQHFRKLLL 93 B*4801 98 1.71 168 1 1 30 6 13 8 QHFRKLLL 94 B*1402 80 1.71 136 1 1 30 6 13 8 QHFRKLLL 94 B*3801 55 1.71 94 1 1 30 6 13 8 QHFRKLLL 94 B*3901 77 1.71 131 1 1 30 4 14 11 SYQHFRKLLLL 95 A*2301 76 1.85 140 1 1 30 4 14 11 SYQHFRKLLLL 95 A*2402 82 1.85 152 1 1 30 5 14 10 YQHFRKLLLL 96 A*0201 36 1.85 67 1 1 30 5 14 10 YQHFRKLLLL 96 B*1402 53 1.85 97 1 1 30 5 14 10 YQHFRKLLLL 96 B*3901 70 1.85 130 1 1 30 5 14 10 YQHFRKLLLL 96 B*4801 85 1.85 156 1 1 30 6 14 9 QHFRKLLLL 97 B*1402 60 1.85 110 1 1 30 6 14 9 QHFRKLLLL 97 B*3801 84 1.85 155 1 1 30 7 14 8 HFRKLLLL 98 B*0801 75 1.85 138 1 1 30 5 15 11 YQHFRKLLLLD 99 B*2705 94 0.80 75 1 1 30 6 16 11 QHFRKLLLLDD 100 B*2705 18 0.57 10 1 1 30 8 18 11 FRKLLLLDDGT 101 B*2705 51 0.12 6 1 1 30 12 20 9 LLLDDGTEA 102 A*0201 24 1.41 34 1 1 30 13 23 11 LLDDGTEAGPL 103 A*0206 33 0.79 26 1 1 30 18 27 10 TEAGPLEEEL 104 B*1301 70 1.36 96 1 1 30 18 27 10 TEAGPLEEEL 104 B*3701 10 1.36 13 1 1 30 18 27 10 TEAGPLEEEL 104 B*3801 35 1.36 47 1 1 30 18 27 10 TEAGPLEEEL 104 B*4002 60 1.36 82 1 1 30 23 30 8 LEEELPRL 105 B*0702 75 1.77 133 1 1 30 23 30 8 LEEELPRL 105 B*1301 69 1.77 122 1 1 30 23 30 8 LEEELPRL 105 B*3701 52 1.77 93 1 1 30 23 30 8 LEEELPRL 105 B*3801 33 1.77 58 1 1 30 23 30 8 LEEELPRL 105 B*4001 74 1.77 131 1 1 30 Cumulative BCI Class I score^(E): 7264 52 61 10 IPWTHKVGNF 106 B*1402 43 1.19 52 2 52 86 52 61 10 IPWTHKVGNF 106 B*3501 47 1.19 55 2 52 86 52 61 10 IPWTHKVGNF 106 B*3503 64 1.19 76 2 52 86 52 61 10 IPWTHKVGNF 106 B*5301 41 1.19 49 2 52 86 52 61 10 IPWTHKVGNF 106 B*5501 41 1.19 48 2 52 86 54 61 8 WTHKVGNF 107 A*2501 84 1.19 100 2 52 86 54 61 8 WTHKVGNF 107 A*2601 82 1.19 98 2 52 86 54 61 8 WTHKVGNF 107 B*4601 44 1.19 53 2 52 86 54 61 8 WTHKVGNF 107 B*5802 10 1.19 12 2 52 86 52 62 11 IPWTHKVGNFT 108 B*5501 50 0.50 25 2 52 86 52 62 11 IPWTHKVGNFT 108 B*5601 60 0.50 30 2 52 86 54 64 11 WTHKVGNFTGL 109 A*2501 80 1.66 132 2 52 86 54 64 11 WTHKVGNFTGL 109 A*2601 64 1.66 107 2 52 86 56 64 9 HKVGNFTGL 110 B*1402 23 1.66 39 2 52 86 56 64 9 HKVGNFTGL 110 B*3901 35 1.66 58 2 52 86 57 64 8 KVGNFTGL 111 A*3201 32 1.66 53 2 52 86 55 65 11 THKVGNFTGLY 112 A*3002 28 1.39 39 2 52 86 56 65 10 HKVGNFTGLY 113 A*2601 23 1.39 32 2 52 86 56 65 10 HKVGNFTGLY 113 A*2902 21 1.39 29 2 52 86 56 65 10 HKVGNFTGLY 113 A*3002 80 1.39 111 2 52 86 57 65 9 KVGNFTGLY 114 A*0101 34 1.39 47 2 52 86 57 65 9 KVGNFTGLY 114 A*0301 39 1.39 55 2 52 86 57 65 9 KVGNFTGLY 114 A*2902 79 1.39 110 2 52 86 57 65 9 KVGNFTGLY 114 A*3002 100 1.39 139 2 52 86 58 65 8 VGNFTGLY 115 A*0101 49 1.39 68 2 52 86 58 65 8 VGNFTGLY 115 A*2902 62 1.39 86 2 52 86 58 65 8 VGNFTGLY 115 A*3002 93 1.39 129 2 52 86 61 71 11 FTGLYSSTVPI 116 A*2501 24 1.12 27 2 52 86 61 71 11 FTGLYSSTVPI 116 A*3201 30 1.12 34 2 52 86 61 71 11 FTGLYSSTVPI 116 A*6802 31 1.12 35 2 52 86 61 71 11 FTGLYSSTVPI 116 B*5101 15 1.12 17 2 52 86 61 71 11 FTGLYSSTVPI 116 B*5201 24 1.12 26 2 52 86 62 71 10 TGLYSSTVPI 117 B*5201 33 1.12 37 2 52 86 63 71 9 GLYSSTVPI 118 A*0201 69 1.12 77 2 52 86 63 71 9 GLYSSTVPI 118 A*3201 88 1.12 99 2 52 86 63 71 9 GLYSSTVPI 118 B*1525 42 1.12 48 2 52 86 63 71 9 GLYSSTVPI 118 B*5201 35 1.12 40 2 52 86 64 71 8 LYSSTVPI 119 A*2301 66 1.12 73 2 52 86 64 71 8 LYSSTVPI 119 A*2402 81 1.12 91 2 52 86 63 72 10 GLYSSTVPIF 120 A*2402 44 1.40 61 2 52 86 63 72 10 GLYSSTVPIF 120 A*3001 74 1.40 104 2 52 86 63 72 10 GLYSSTVPIF 120 B*1501 95 1.40 133 2 52 86 63 72 10 GLYSSTVPIF 120 B*1502 80 1.40 112 2 52 86 63 72 10 GLYSSTVPIF 120 B*1525 92 1.40 128 2 52 86 64 72 9 LYSSTVPIF 121 A*2301 79 1.40 111 2 52 86 64 72 9 LYSSTVPIF 121 A*2402 98 1.40 138 2 52 86 65 72 8 YSSTVPIF 122 A*0101 26 1.40 37 2 52 86 65 72 8 YSSTVPIF 122 B*4601 85 1.40 119 2 52 86 65 72 8 YSSTVPIF 122 B*5301 59 1.40 83 2 52 86 65 72 8 YSSTVPIF 122 B*5701 56 1.40 79 2 52 86 65 72 8 YSSTVPIF 122 B*5801 80 1.40 112 2 52 86 65 72 8 YSSTVPIF 122 B*5802 77 1.40 108 2 52 86 65 74 10 YSSTVPIFNP 123 B*5701 98 0.65 64 2 52 86 65 74 10 YSSTVPIFNP 123 B*5801 85 0.65 55 2 52 86 66 76 11 SSTVPIFNPEW 124 B*5701 100 1.48 148 2 52 86 66 76 11 SSTVPIFNPEW 124 B*5801 97 1.48 143 2 52 86 66 76 11 SSTVPIFNPEW 124 B*5802 93 1.48 137 2 52 86 67 76 10 STVPIFNPEW 125 B*4402 19 1.48 28 2 52 86 67 76 10 STVPIFNPEW 125 B*4403 64 1.48 95 2 52 86 67 76 10 STVPIFNPEW 125 B*5802 91 1.48 135 2 52 86 69 76 8 VPIFNPEW 126 B*3503 5 1.48 8 2 52 86 69 76 8 VPIFNPEW 126 B*5101 32 1.48 47 2 52 86 69 76 8 VPIFNPEW 126 B*5301 90 1.48 133 2 52 86 70 79 10 PIFNPEWQTP 127 A*3201 36 0.51 19 2 52 86 71 81 11 IFNPEWQTPSF 128 A*2301 95 1.19 112 2 52 86 71 81 11 IFNPEWQTPSF 128 A*2402 79 1.19 94 2 52 86 73 81 9 NPEWQTPSF 129 B*0702 55 1.19 65 2 52 86 73 81 9 NPEWQTPSF 129 B*3501 92 1.19 109 2 52 86 73 81 9 NPEWQTPSF 129 B*3503 62 1.19 74 2 52 86 73 81 9 NPEWQTPSF 129 B*5301 84 1.19 99 2 52 86 74 81 8 PEWQTPSF 130 B*1801 71 1.19 85 2 52 86 74 81 8 PEWQTPSF 130 B*4402 62 1.19 73 2 52 86 74 81 8 PEWQTPSF 130 B*4403 72 1.19 85 2 52 86 76 83 8 WQTPSFPK 131 A*1101 7 0.81 5 2 52 86 74 84 11 PEWQTPSFPKI 132 B*1301 82 1.32 108 2 52 86 74 84 11 PEWQTPSFPKI 132 B*1302 15 1.32 20 2 52 86 74 84 11 PEWQTPSFPKI 132 B*4001 4 1.32 6 2 52 86 74 84 11 PEWQTPSFPKI 132 B*4402 31 1.32 41 2 52 86 74 84 11 PEWQTPSFPKI 132 B*4403 36 1.32 48 2 52 86 74 84 11 PEWQTPSFPKI 132 B*4901 78 1.32 103 2 52 86 76 84 9 WQTPSFPKI 133 A*0206 67 1.32 88 2 52 86 76 84 9 WQTPSFPKI 133 B*1301 99 1.32 130 2 52 86 76 84 9 WQTPSFPKI 133 B*1302 51 1.32 67 2 52 86 76 84 9 WQTPSFPKI 133 B*3701 38 1.32 50 2 52 86 76 84 9 WQTPSFPKI 133 B*4801 10 1.32 13 2 52 86 76 84 9 WQTPSFPKI 133 B*4901 17 1.32 23 2 52 86 76 84 9 WQTPSFPKI 133 B*5201 100 1.32 132 2 52 86 76 86 11 WQTPSFPKIHL 134 B*1301 86 1.51 130 2 52 86 76 86 11 WQTPSFPKIHL 134 B*1302 14 1.51 21 2 52 86 76 86 11 WQTPSFPKIHL 134 B*3701 33 1.51 50 2 52 86 76 86 11 WQTPSFPKIHL 134 B*3801 59 1.51 89 2 52 86 76 86 11 WQTPSFPKIHL 134 B*3901 44 1.51 67 2 52 86 76 86 11 WQTPSFPKIHL 134 B*4001 30 1.51 46 2 52 86 76 86 11 WQTPSFPKIHL 134 B*4801 83 1.51 125 2 52 86 78 86 9 TPSFPKIHL 135 B*0702 10 1.51 15 2 52 86 Cumulative BCI Class I score: 6943 104 111 8 NEKRRLKL 136 B*0801 83 1.27 105 3 103 135 104 112 9 NEKRRLKLI 137 B*4402 42 0.71 30 3 103 135 104 112 9 NEKRRLKLI 137 B*4901 4 0.71 3 3 103 135 106 113 8 KRRLKLIM 138 B*2702 69 0.90 62 3 103 135 106 113 8 KRRLKLIM 138 B*2705 49 0.90 44 3 103 135 107 114 8 RRLKLIMP 139 B*2702 39 0.23 9 3 103 135 107 114 8 RRLKLIMP 139 B*2705 100 0.23 23 3 103 135 106 115 10 KRRLKLIMPA 140 B*2705 16 1.60 26 3 103 135 107 115 9 RRLKLIMPA 141 B*2702 93 1.60 148 3 103 135 107 115 9 RRLKLIMPA 141 B*2705 99 1.60 157 3 103 135 108 115 8 RLKLIMPA 142 A*3001 52 1.60 83 3 103 135 108 115 8 RLKLIMPA 142 B*0801 46 1.60 73 3 103 135 106 116 11 KRRLKLIMPAR 143 B*2705 42 0.86 36 3 103 135 107 116 10 RRLKLIMPAR 144 A*3101 49 0.86 42 3 103 135 107 116 10 RRLKLIMPAR 144 B*2702 63 0.86 54 3 103 135 107 116 10 RRLKLIMPAR 144 B*2705 97 0.86 83 3 103 135 108 116 9 RLKLIMPAR 145 A*3101 96 0.86 83 3 103 135 108 116 9 RLKLIMPAR 145 A*3303 61 0.86 52 3 103 135 108 116 9 RLKLIMPAR 145 A*7401 91 0.86 78 3 103 135 107 117 11 RRLKLIMPARF 146 B*2705 78 1.18 91 3 103 135 108 117 10 RLKLIMPARF 147 B*1501 16 1.18 18 3 103 135 110 117 8 KLIMPARF 148 A*2301 9 1.18 10 3 103 135 110 117 8 KLIMPARF 148 A*3201 95 1.18 112 3 103 135 110 117 8 KLIMPARF 148 B*1501 55 1.18 64 3 103 135 110 117 8 KLIMPARF 148 B*1525 58 1.18 68 3 103 135 108 118 11 RLKLIMPARFY 149 A*0301 34 1.43 49 3 103 135 108 118 11 RLKLIMPARFY 149 A*3001 32 1.43 45 3 103 135 108 118 11 RLKLIMPARFY 149 A*3002 92 1.43 131 3 103 135 108 118 11 RLKLIMPARFY 149 B*1501 14 1.43 20 3 103 135 109 118 10 LKLIMPARFY 150 A*2902 35 1.43 50 3 103 135 110 118 9 KLIMPARFY 151 A*0301 38 1.43 54 3 103 135 110 118 9 KLIMPARFY 151 A*3002 75 1.43 107 3 103 135 111 118 8 LIMPARFY 152 A*2902 71 1.43 102 3 103 135 111 118 8 LIMPARFY 152 A*3002 68 1.43 97 3 103 135 111 118 8 LIMPARFY 152 B*1501 45 1.43 65 3 103 135 111 118 8 LIMPARFY 152 B*1502 50 1.43 71 3 103 135 111 118 8 LIMPARFY 152 B*1525 27 1.43 39 3 103 135 111 118 8 LIMPARFY 152 B*3501 24 1.43 34 3 103 135 111 120 10 LIMPARFYPT 153 A*0206 77 0.18 13 3 103 135 113 120 8 MPARFYPT 154 A*6802 21 0.18 4 3 103 135 113 120 8 MPARFYPT 154 B*0801 58 0.18 10 3 103 135 113 120 8 MPARFYPT 154 B*1402 35 0.18 6 3 103 135 113 120 8 MPARFYPT 154 B*3503 80 0.18 14 3 103 135 113 120 8 MPARFYPT 154 B*5101 75 0.18 13 3 103 135 113 120 8 MPARFYPT 154 B*5301 23 0.18 4 3 103 135 113 120 8 MPARFYPT 154 B*5501 100 0.18 18 3 103 135 113 121 9 MPARFYPTH 155 B*3501 84 1.01 85 3 103 135 113 121 9 MPARFYPTH 155 B*3503 23 1.01 23 3 103 135 113 121 9 MPARFYPTH 155 B*5301 62 1.01 63 3 103 135 113 121 9 MPARFYPTH 155 B*5501 57 1.01 58 3 103 135 113 121 9 MPARFYPTH 155 B*5601 45 1.01 45 3 103 135 113 122 10 MPARFYPTHT 156 B*3501 23 0.98 22 3 103 135 113 122 10 MPARFYPTHT 156 B*3503 19 0.98 19 3 103 135 113 122 10 MPARFYPTHT 156 B*5301 10 0.98 10 3 103 135 113 122 10 MPARFYPTHT 156 B*5501 73 0.98 72 3 103 135 113 122 10 MPARFYPTHT 156 B*5601 81 0.98 79 3 103 135 115 122 8 ARFYPTHT 157 B*2705 15 0.98 15 3 103 135 113 123 11 MPARFYPTHTK 158 B*5501 49 1.38 67 3 103 135 113 123 11 MPARFYPTHTK 158 B*5601 54 1.38 74 3 103 135 115 123 9 ARFYPTHTK 159 B*2705 87 1.38 119 3 103 135 116 123 8 RFYPTHTK 160 A*0301 84 1.38 115 3 103 135 116 123 8 RFYPTHTK 160 A*3001 79 1.38 109 3 103 135 116 123 8 RFYPTHTK 160 A*3101 76 1.38 105 3 103 135 116 123 8 RFYPTHTK 160 A*7401 57 1.38 79 3 103 135 115 124 10 ARFYPTHTKY 161 A*2902 6 1.50 10 3 103 135 115 124 10 ARFYPTHTKY 161 B*2702 61 1.50 92 3 103 135 115 124 10 ARFYPTHTKY 161 B*2705 55 1.50 83 3 103 135 116 124 9 RFYPTHTKY 162 A*2902 92 1.50 138 3 103 135 116 124 9 RFYPTHTKY 162 A*3002 1 1.50 2 3 103 135 117 124 8 FYPTHTKY 163 B*3501 51 1.50 76 3 103 135 115 125 11 ARFYPTHTKYL 164 B*2702 67 1.93 130 3 103 135 115 125 11 ARFYPTHTKYL 164 B*2705 34 1.93 66 3 103 135 116 125 10 RFYPTHTKYL 165 B*4801 4 1.93 7 3 103 135 117 125 9 FYPTHTKYL 166 A*2402 39 1.93 74 3 103 135 118 125 8 YPTHTKYL 167 B*1402 42 1.93 82 3 103 135 118 125 8 YPTHTKYL 167 B*3501 17 1.93 33 3 103 135 118 125 8 YPTHTKYL 167 B*3503 78 1.93 151 3 103 135 118 125 8 YPTHTKYL 167 B*5101 43 1.93 83 3 103 135 118 125 8 YPTHTKYL 167 B*5301 51 1.93 98 3 103 135 118 125 8 YPTHTKYL 167 B*5501 31 1.93 60 3 103 135 117 126 10 FYPTHTKYLP 168 A*2402 54 0.14 7 3 103 135 118 126 9 YPTHTKYLP 169 B*5301 2 0.14 0 3 103 135 117 127 11 FYPTHTKYLPL 170 A*2301 52 0.94 49 3 103 135 117 127 11 FYPTHTKYLPL 170 A*2402 56 0.94 53 3 103 135 118 127 10 YPTHTKYLPL 171 B*0702 65 0.94 61 3 103 135 118 127 10 YPTHTKYLPL 171 B*1402 100 0.94 94 3 103 135 118 127 10 YPTHTKYLPL 171 B*3501 75 0.94 70 3 103 135 118 127 10 YPTHTKYLPL 171 B*3503 100 0.94 94 3 103 135 118 127 10 YPTHTKYLPL 171 B*3901 96 0.94 90 3 103 135 118 127 10 YPTHTKYLPL 171 B*5101 83 0.94 78 3 103 135 118 127 10 YPTHTKYLPL 171 B*5301 82 0.94 77 3 103 135 118 127 10 YPTHTKYLPL 171 B*5501 87 0.94 82 3 103 135 118 127 10 YPTHTKYLPL 171 B*5601 67 0.94 63 3 103 135 120 127 8 THTKYLPL 172 B*1402 95 0.94 89 3 103 135 120 127 8 THTKYLPL 172 B*3801 80 0.94 75 3 103 135 119 128 10 PTHTKYLPLD 173 A*3001 46 0.71 33 3 103 135 121 129 9 HTKYLPLDK 174 A*0301 18 0.41 7 3 103 135 121 129 9 HTKYLPLDK 174 A*3001 90 0.41 37 3 103 135 123 131 9 KYLPLDKGI 175 A*2301 34 1.23 43 3 103 135 123 131 9 KYLPLDKGI 175 A*2402 21 1.23 26 3 103 135 125 132 8 LPLDKGIK 176 B*3501 56 0.80 45 3 103 135 125 134 10 LPLDKGIKPY 177 B*3501 87 1.08 94 3 103 135 125 134 10 LPLDKGIKPY 177 B*3503 36 1.08 39 3 103 135 125 134 10 LPLDKGIKPY 177 B*5301 39 1.08 43 3 103 135 125 134 10 LPLDKGIKPY 177 B*5501 13 1.08 14 3 103 135 126 134 9 PLDKGIKPY 178 A*0101 25 1.08 27 3 103 135 127 134 8 LDKGIKPY 179 B*3501 9 1.08 10 3 103 135 125 135 11 LPLDKGIKPYY 180 B*3501 77 1.16 90 3 103 135 125 135 11 LPLDKGIKPYY 180 B*5301 57 1.16 67 3 103 135 126 135 10 PLDKGIKPYY 181 A*0101 55 1.16 64 3 103 135 126 135 10 PLDKGIKPYY 181 A*2902 3 1.16 4 3 103 135 Cumulative Class I-BCI score: 6469 118 127 10 YPTHTKYLPL 171 B*0702 65 0.94 61 4 118 150 118 127 10 YPTHTKYLPL 171 B*1402 100 0.94 94 4 118 150 118 127 10 YPTHTKYLPL 171 B*3501 75 0.94 70 4 118 150 118 127 10 YPTHTKYLPL 171 B*3503 100 0.94 94 4 118 150 118 127 10 YPTHTKYLPL 171 B*3901 96 0.94 90 4 118 150 118 127 10 YPTHTKYLPL 171 B*5101 83 0.94 78 4 118 150 118 127 10 YPTHTKYLPL 171 B*5301 82 0.94 77 4 118 150 118 127 10 YPTHTKYLPL 171 B*5501 87 0.94 82 4 118 150 118 127 10 YPTHTKYLPL 171 B*5601 67 0.94 63 4 118 150 120 127 8 THTKYLPL 172 B*1402 95 0.94 89 4 118 150 120 127 8 THTKYLPL 172 B*3801 80 0.94 75 4 118 150 119 128 10 PTHTKYLPLD 173 A*3001 46 0.71 33 4 118 150 121 129 9 HTKYLPLDK 174 A*0301 18 0.41 7 4 118 150 121 129 9 HTKYLPLDK 174 A*3001 90 0.41 37 4 118 150 123 131 9 KYLPLDKGI 175 A*2301 34 1.23 43 4 118 150 123 131 9 KYLPLDKGI 175 A*2402 21 1.23 26 4 118 150 125 132 8 LPLDKGIK 176 B*3501 56 0.80 45 4 118 150 125 134 10 LPLDKGIKPY 177 B*3501 87 1.08 94 4 118 150 125 134 10 LPLDKGIKPY 177 B*3503 36 1.08 39 4 118 150 125 134 10 LPLDKGIKPY 177 B*5301 39 1.08 43 4 118 150 125 134 10 LPLDKGIKPY 177 B*5501 13 1.08 14 4 118 150 126 134 9 PLDKGIKPY 178 A*0101 25 1.08 27 4 118 150 127 134 8 LDKGIKPY 179 B*3501 9 1.08 10 4 118 150 125 135 11 LPLDKGIKPYY 180 B*3501 77 1.16 90 4 118 150 125 135 11 LPLDKGIKPYY 180 B*5301 57 1.16 67 4 118 150 126 135 10 PLDKGIKPYY 181 A*0101 55 1.16 64 4 118 150 126 135 10 PLDKGIKPYY 181 A*2902 3 1.16 4 4 118 150 132 139 8 KPYYPDQV 182 B*5101 65 1.05 68 4 118 150 132 139 8 KPYYPDQV 182 B*5501 64 1.05 67 4 118 150 132 139 8 KPYYPDQV 182 B*5601 59 1.05 62 4 118 150 132 140 9 KPYYPDQVV 183 B*0702 36 1.80 65 4 118 150 132 140 9 KPYYPDQVV 183 B*5101 70 1.80 126 4 118 150 132 140 9 KPYYPDQVV 183 B*5501 86 1.80 155 4 118 150 132 140 9 KPYYPDQVV 183 B*5601 65 1.80 118 4 118 150 135 142 8 YPDQVVNH 184 B*3501 89 1.63 146 4 118 150 134 143 10 YYPDQVVNHY 185 A*0101 23 1.33 30 4 118 150 134 143 10 YYPDQVVNHY 185 A*2402 25 1.33 33 4 118 150 134 143 10 YYPDQVVNHY 185 A*2902 65 1.33 87 4 118 150 134 143 10 YYPDQVVNHY 185 A*3002 25 1.33 34 4 118 150 135 143 9 YPDQVVNHY 186 A*0101 62 1.33 83 4 118 150 135 143 9 YPDQVVNHY 186 B*3501 83 1.33 110 4 118 150 135 143 9 YPDQVVNHY 186 B*3503 55 1.33 74 4 118 150 135 143 9 YPDQVVNHY 186 B*5301 44 1.33 59 4 118 150 136 143 8 PDQVVNHY 187 B*3501 4 1.33 5 4 118 150 134 144 11 YYPDQVVNHYF 188 A*2301 100 1.77 177 4 118 150 135 144 10 YPDQVVNHYF 189 B*3501 100 1.77 177 4 118 150 135 144 10 YPDQVVNHYF 189 B*3503 95 1.77 168 4 118 150 135 144 10 YPDQVVNHYF 189 B*5301 100 1.77 177 4 118 150 137 144 8 DQVVNHYF 190 B*1801 52 1.77 93 4 118 150 137 147 11 DQVVNHYFQTR 191 A*3303 21 1.63 34 4 118 150 138 147 10 QVVNHYFQTR 192 A*3101 1 1.63 2 4 118 150 138 147 10 QVVNHYFQTR 192 A*3303 86 1.63 140 4 118 150 138 147 10 QVVNHYFQTR 192 A*6801 68 1.63 110 4 118 150 138 147 10 QVVNHYFQTR 192 A*7401 17 1.63 28 4 118 150 139 147 9 VVNHYFQTR 193 A*3101 87 1.63 143 4 118 150 139 147 9 VVNHYFQTR 193 A*3303 73 1.63 120 4 118 150 139 147 9 VVNHYFQTR 193 A*7401 72 1.63 117 4 118 150 139 149 11 VVNHYFQTRHY 194 A*0101 42 1.90 79 4 118 150 139 149 11 VVNHYFQTRHY 194 A*2902 70 1.90 133 4 118 150 139 149 11 VVNHYFQTRHY 194 A*3002 90 1.90 172 4 118 150 139 149 11 VVNHYFQTRHY 194 B*1501 50 1.90 95 4 118 150 139 149 11 VVNHYFQTRHY 194 B*1502 44 1.90 85 4 118 150 141 149 9 NHYFQTRHY 195 B*3801 16 1.90 31 4 118 150 142 149 8 HYFQTRHY 196 A*2902 25 1.90 48 4 118 150 142 149 8 HYFQTRHY 196 A*3002 44 1.90 83 4 118 150 141 150 10 NHYFQTRHYL 197 B*1402 94 1.93 181 4 118 150 141 150 10 NHYFQTRHYL 197 B*3801 53 1.93 102 4 118 150 141 150 10 NHYFQTRHYL 197 B*3901 88 1.93 170 4 118 150 142 150 9 HYFQTRHYL 198 A*2301 69 1.93 133 4 118 150 142 150 9 HYFQTRHYL 198 B*1402 34 1.93 66 4 118 150 142 150 9 HYFQTRHYL 198 B*3901 3 1.93 5 4 118 150 143 150 8 YFQTRHYL 199 A*2301 74 1.93 143 4 118 150 143 150 8 YFQTRHYL 199 A*2402 74 1.93 142 4 118 150 143 150 8 YFQTRHYL 199 B*0801 93 1.93 180 4 118 150 Cumulative Class I-BCI score: 6169 139 149 11 VVNHYFQTRHY 194 A*0101 42 1.90 79 5 139 177 139 149 11 VVNHYFQTRHY 194 A*2902 70 1.90 133 5 139 177 139 149 11 VVNHYFQTRHY 194 A*3002 90 1.90 172 5 139 177 139 149 11 VVNHYFQTRHY 194 B*1501 50 1.90 95 5 139 177 139 149 11 VVNHYFQTRHY 194 B*1502 44 1.90 85 5 139 177 141 149 9 NHYFQTRHY 195 B*3801 16 1.90 31 5 139 177 142 149 8 HYFQTRHY 196 A*2902 25 1.90 48 5 139 177 142 149 8 HYFQTRHY 196 A*3002 44 1.90 83 5 139 177 141 150 10 NHYFQTRHYL 197 B*1402 94 1.93 181 5 139 177 141 150 10 NHYFQTRHYL 197 B*3801 53 1.93 102 5 139 177 141 150 10 NHYFQTRHYL 197 B*3901 88 1.93 170 5 139 177 142 150 9 HYFQTRHYL 198 A*2301 69 1.93 133 5 139 177 142 150 9 HYFQTRHYL 198 B*1402 34 1.93 66 5 139 177 142 150 9 HYFQTRHYL 198 B*3901 3 1.93 5 5 139 177 143 150 8 YFQTRHYL 199 A*2301 74 1.93 143 5 139 177 143 150 8 YFQTRHYL 199 A*2402 74 1.93 142 5 139 177 143 150 8 YFQTRHYL 199 B*0801 93 1.93 180 5 139 177 142 151 10 HYFQTRHYLH 200 A*2301 33 0.39 13 5 139 177 142 151 10 HYFQTRHYLH 200 A*2402 49 0.39 19 5 139 177 142 151 10 HYFQTRHYLH 200 A*2902 16 0.39 6 5 139 177 143 151 9 YFQTRHYLH 201 A*2902 57 0.39 22 5 139 177 143 153 11 YFQTRHYLHTL 202 A*2301 98 1.22 120 5 139 177 143 153 11 YFQTRHYLHTL 202 A*2402 100 1.22 122 5 139 177 143 153 11 YFQTRHYLHTL 202 B*0801 100 1.22 122 5 139 177 144 153 10 FQTRhYLHTL 203 A*0201 27 1.22 33 5 139 177 144 153 10 FQTRHYLHTL 203 B*1301 63 1.22 77 5 139 177 144 153 10 FQTRHYLHTL 203 B*1402 52 1.22 63 5 139 177 144 153 10 FQTRHYLHTL 203 B*3701 62 1.22 75 5 139 177 144 153 10 FQTRHYLHTL 203 B*3801 71 1.22 87 5 139 177 144 153 10 FQTRHYLHTL 203 B*3901 94 1.22 114 5 139 177 144 153 10 FQTRHYLHTL 203 B*4801 81 1.22 98 5 139 177 145 153 9 QTRHYLHTL 204 A*2501 65 1.22 79 5 139 177 146 153 8 TRHYLHTL 205 B*1402 72 1.22 87 5 139 177 146 153 8 TRHYLHTL 205 B*2702 60 1.22 73 5 139 177 146 153 8 TRHYLHTL 205 B*2705 70 1.22 85 5 139 177 144 154 11 FQTRHYLHTLW 206 B*1301 68 1.50 101 5 139 177 144 154 11 FQTRHYLHTLW 206 B*2702 37 1.50 56 5 139 177 145 154 10 QTRHYLHTLW 207 B*4402 35 1.50 52 5 139 177 145 154 10 QTRHYLHTLW 207 B*5802 70 1.50 104 5 139 177 146 154 9 TRHYLHTLW 208 B*2702 76 1.50 114 5 139 177 147 154 8 RHYLHTLW 209 A*2301 47 1.50 70 5 139 177 147 154 8 RHYLHTLW 209 A*2402 35 1.50 52 5 139 177 147 154 8 RHYLHTLW 209 B*2702 99 1.50 148 5 139 177 147 154 8 RHYLHTLW 209 B*3801 98 1.50 147 5 139 177 147 154 8 RHYLHTLW 209 B*5701 35 1.50 52 5 139 177 147 154 8 RHYLHTLW 209 B*5801 22 1.50 33 5 139 177 147 154 8 RHYLHTLW 209 B*5802 26 1.50 39 5 139 177 145 155 11 QTRHYLHTLWK 210 A*0301 54 0.72 39 5 139 177 145 155 11 QTRHYLHTLWK 210 A*1101 35 0.72 25 5 139 177 145 155 11 QTRHYLHTLWK 210 A*3001 96 0.72 69 5 139 177 146 155 10 TRHYLHTLWK 211 B*2705 36 0.72 26 5 139 177 147 155 9 RHYLHTLWK 212 A*0301 70 0.72 51 5 139 177 147 155 9 RHYLHTLWK 212 B*2702 7 0.72 5 5 139 177 148 155 8 HYLHTLWK 213 A*3101 29 0.72 21 5 139 177 146 156 11 TRHYLHTLWKA 214 B*2705 58 1.23 72 5 139 177 148 156 9 HYLHTLWKA 215 A*2301 31 1.23 38 5 139 177 147 157 11 RHYLHTLWKAG 216 B*2705 6 0.73 4 5 139 177 148 157 10 HYLHTLWKAG 217 A*3201 74 0.73 54 5 139 177 148 158 11 HYLHTLWKAGI 218 A*2301 93 0.63 59 5 139 177 148 158 11 HYLHTLWKAGI 218 A*2402 95 0.63 60 5 139 177 149 158 10 YLHTLWKAGI 219 A*0201 7 0.63 4 5 139 177 151 158 8 HTLWKAGI 220 A*3201 62 0.63 39 5 139 177 149 159 11 YLHTLWKAGIL 221 B*0801 88 0.85 75 5 139 177 149 159 11 YLHTLWKAGIL 221 B*3901 22 0.85 19 5 139 177 150 159 10 LHTLWKAGIL 222 B*0801 69 0.85 59 5 139 177 150 159 10 LHTLWKAGIL 222 B*3801 51 0.85 43 5 139 177 150 159 10 LHTLWKAGIL 222 B*3901 34 0.85 29 5 139 177 151 159 9 HTLWKAGIL 223 B*5802 1 0.85 1 5 139 177 151 160 10 HTLWKAGILY 224 A*0101 72 1.87 134 5 139 177 151 160 10 HTLWKAGILY 224 A*0301 7 1.87 12 5 139 177 151 160 10 HTLWKAGILY 224 A*2501 47 1.87 88 5 139 177 151 160 10 HTLWKAGILY 224 A*2601 67 1.87 125 5 139 177 151 160 10 HTLWKAGILY 224 A*2902 2 1.87 3 5 139 177 151 160 10 HTLWKAGILY 224 A*3002 49 1.87 92 5 139 177 152 160 9 TLWKAGILY 225 A*0301 36 1.87 67 5 139 177 152 160 9 TLWKAGILY 225 A*2902 78 1.87 145 5 139 177 152 160 9 TLWKAGILY 225 A*3002 4 1.87 8 5 139 177 153 160 8 LWKAGILY 226 A*2902 56 1.87 104 5 139 177 153 160 8 LWKAGILY 226 A*3002 85 1.87 158 5 139 177 153 160 8 LWKAGILY 226 B*3501 8 1.87 15 5 139 177 151 161 11 HTLWKAGILYK 227 A*0301 89 1.41 125 5 139 177 151 161 11 HTLWKAGILYK 227 A*1101 100 1.41 141 5 139 177 151 161 11 HTLWKAGILYK 227 A*3001 78 1.41 110 5 139 177 151 161 11 HTLWKAGILYK 227 A*3101 46 1.41 64 5 139 177 151 161 11 HTLWKAGILYK 227 A*3303 25 1.41 36 5 139 177 151 161 11 HTLWKAGILYK 227 A*6801 75 1.41 106 5 139 177 151 161 11 HTLWKAGILYK 227 A*7401 83 1.41 117 5 139 177 152 161 10 TLWKAGILYK 228 A*0301 87 1.41 122 5 139 177 152 161 10 TLWKAGILYK 228 A*1101 59 1.41 83 5 139 177 152 161 10 TLWKAGILYK 228 A*7401 71 1.41 100 5 139 177 153 161 9 LWKAGILYK 229 A*3001 57 1.41 80 5 139 177 152 162 11 TLWKAGILYKR 230 A*3101 61 1.49 91 5 139 177 152 162 11 TLWKAGILYKR 230 A*3303 72 1.49 107 5 139 177 152 162 11 TLWKAGILYKR 230 A*7401 82 1.49 122 5 139 177 153 162 10 LWKAGILYKR 231 A*3101 86 1.49 128 5 139 177 153 162 10 LWKAGILYKR 231 A*3303 59 1.49 88 5 139 177 155 162 8 KAGILYKR 232 A*3101 67 1.49 100 5 139 177 155 162 8 KAGILYKR 232 A*7401 27 1.49 40 5 139 177 158 166 9 ILYKRETTR 233 A*0301 66 1.75 115 5 139 177 158 166 9 ILYKRETTR 233 A*3101 23 1.75 40 5 139 177 158 166 9 ILYKRETTR 233 A*3303 51 1.75 89 5 139 177 158 166 9 ILYKRETTR 233 A*7401 90 1.75 158 5 139 177 158 168 11 ILYKRETTRSA 234 B*0801 56 1.80 100 5 139 177 160 170 11 YKRETTRSASF 235 B*0702 17 1.82 32 5 139 177 160 170 11 YKRETTRSASF 235 B*0801 81 1.82 148 5 139 177 160 170 11 YKRETTRSASF 235 B*1402 68 1.82 123 5 139 177 160 170 11 YKRETTRSASF 235 B*1501 53 1.82 97 5 139 177 160 170 11 YKRETTRSASF 235 B*1502 65 1.82 118 5 139 177 160 170 11 YKRETTRSASF 235 B*1525 46 1.82 83 5 139 177 161 170 10 KRETTRSASF 236 B*2702 53 1.82 97 5 139 177 162 170 9 RETTRSASF 237 B*4001 57 1.82 103 5 139 177 162 170 9 RETTRSASF 237 B*4402 88 1.82 161 5 139 177 162 170 9 RETTRSASF 237 B*4403 60 1.82 109 5 139 177 162 170 9 RETTRSASF 237 B*5001 44 1.82 80 5 139 177 163 170 8 ETTRSASF 238 A*2501 100 1.82 182 5 139 177 163 170 8 ETTRSASF 238 A*2601 100 1.82 182 5 139 177 166 175 10 RSASFCGSPY 239 A*0101 79 1.16 92 5 139 177 166 175 10 RSASFCGSPY 239 A*2501 45 1.16 52 5 139 177 166 175 10 RSASFCGSPY 239 B*1501 94 1.16 108 5 139 177 166 175 10 RSASFCGSPY 239 B*1502 78 1.16 90 5 139 177 166 175 10 RSASFCGSPY 239 B*1525 80 1.16 92 5 139 177 166 175 10 RSASFCGSPY 239 B*4403 32 1.16 37 5 139 177 166 175 10 RSASFCGSPY 239 B*4601 84 1.16 97 5 139 177 166 175 10 RSASFCGSPY 239 B*5802 68 1.16 79 5 139 177 167 175 9 SASFCGSPY 240 A*3002 79 1.16 91 5 139 177 167 175 9 SASFCGSPY 240 B*3501 81 1.16 94 5 139 177 168 175 8 ASFCGSPY 241 A*1101 70 1.16 80 5 139 177 168 175 8 ASFCGSPY 241 A*2902 54 1.16 62 5 139 177 168 175 8 ASFCGSPY 241 B*5701 44 1.16 51 5 139 177 167 176 10 SASFCGSPYS 242 A*3001 8 0.16 1 5 139 177 167 176 10 SASFCGSPYS 242 B*5701 76 0.16 12 5 139 177 167 176 10 SASFCGSPYS 242 B*5801 76 0.16 12 5 139 177 168 176 9 ASFCGSPYS 243 B*5802 19 0.16 3 5 139 177 167 177 11 SASFCGSPYSW 244 B*5301 79 1.90 150 5 139 177 167 177 11 SASFCGSPYSW 244 B*5701 94 1.90 179 5 139 177 167 177 11 SASFCGSPYSW 244 B*5801 100 1.90 190 5 139 177 167 177 11 SASFCGSPYSW 244 B*5802 100 1.90 190 5 139 177 168 177 10 ASFCGSPYSW 245 B*4402 69 1.90 132 5 139 177 168 177 10 ASFCGSPYSW 245 B*4403 28 1.90 53 5 139 177 168 177 10 ASFCGSPYSW 245 B*5802 99 1.90 188 5 139 177 169 177 9 SFCGSPYSW 246 A*2301 26 1.90 49 5 139 177 Cumulative BCI Class Iscore: 11815 143 150 8 YFQTRHYL 199 A*2301 74 1.93 143 6 143 177 143 150 8 YFQTRHYL 199 A*2402 74 1.93 142 6 143 177 143 150 8 YFQTRHYL 199 B*0801 93 1.93 180 6 143 177 142 151 10 HYFQTRHYLH 200 A*2301 33 0.39 13 6 143 177 142 151 10 HYFQTRHYLH 200 A*2402 49 0.39 19 6 143 177 142 151 10 HYFQTRHYLH 200 A*2902 16 0.39 6 6 143 177 143 151 9 YFQTRHYLH 201 A*2902 57 0.39 22 6 143 177 143 153 11 YFQTRHYLHTL 202 A*2301 98 1.22 120 6 143 177 143 153 11 YFQTRHYLHTL 202 A*2402 100 1.22 122 6 143 177 143 153 11 YFQTRHYLHTL 202 B*0801 100 1.22 122 6 143 177 144 153 10 FQTRhYLHTL 203 A*0201 27 1.22 33 6 143 177 144 153 10 FQTRHYLHTL 203 B*1301 63 1.22 77 6 143 177 144 153 10 FQTRHYLHTL 203 B*1402 52 1.22 63 6 143 177 144 153 10 FQTRHYLHTL 203 B*3701 62 1.22 75 6 143 177 144 153 10 FQTRHYLHTL 203 B*3801 71 1.22 87 6 143 177 144 153 10 FQTRHYLHTL 203 B*3901 94 1.22 114 6 143 177 144 153 10 FQTRHYLHTL 203 B*4801 81 1.22 98 6 143 177 145 153 9 QTRHYLHTL 204 A*2501 65 1.22 79 6 143 177 146 153 8 TRHYLHTL 205 B*1402 72 1.22 87 6 143 177 146 153 8 TRHYLHTL 205 B*2702 60 1.22 73 6 143 177 146 153 8 TRHYLHTL 205 B*2705 70 1.22 85 6 143 177 144 154 11 FQTRHYLHTLW 206 B*1301 68 1.50 101 6 143 177 144 154 11 FQTRHYLHTLW 206 B*2702 37 1.50 56 6 143 177 145 154 10 QTRHYLHTLW 207 B*4402 35 1.50 52 6 143 177 145 154 10 QTRHYLHTLW 207 B*5802 70 1.50 104 6 143 177 146 154 9 TRHYLHTLW 208 B*2702 76 1.50 114 6 143 177 147 154 8 RHYLHTLW 209 A*2301 47 1.50 70 6 143 177 147 154 8 RHYLHTLW 209 A*2402 35 1.50 52 6 143 177 147 154 8 RHYLHTLW 209 B*2702 99 1.50 148 6 143 177 147 154 8 RHYLHTLW 209 B*3801 98 1.50 147 6 143 177 147 154 8 RHYLHTLW 209 B*5701 35 1.50 52 6 143 177 147 154 8 RHYLHTLW 209 B*5801 22 1.50 33 6 143 177 147 154 8 RHYLHTLW 209 B*5802 26 1.50 39 6 143 177 145 155 11 QTRHYLHTLWK 210 A*0301 54 0.72 39 6 143 177 145 155 11 QTRHYLHTLWK 210 A*1101 35 0.72 25 6 143 177 145 155 11 QTRHYLHTLWK 210 A*3001 96 0.72 69 6 143 177 146 155 10 TRHYLHTLWK 211 B*2705 36 0.72 26 6 143 177 147 155 9 RHYLHTLWK 212 A*0301 70 0.72 51 6 143 177 147 155 9 RHYLHTLWK 212 B*2702 7 0.72 5 6 143 177 148 155 8 HYLHTLWK 213 A*3101 29 0.72 21 6 143 177 146 156 11 TRHYLHTLWKA 214 B*2705 58 1.23 72 6 143 177 148 156 9 HYLHTLWKA 215 A*2301 31 1.23 38 6 143 177 147 157 11 RHYLHTLWKAG 216 B*2705 6 0.73 4 6 143 177 148 157 10 HYLHTLWKAG 217 A*3201 74 0.73 54 6 143 177 148 158 11 HYLHTLWKAGI 218 A*2301 93 0.63 59 6 143 177 148 158 11 HYLHTLWKAGI 218 A*2402 95 0.63 60 6 143 177 149 158 10 YLHTLWKAGI 219 A*0201 7 0.63 4 6 143 177 151 158 8 HTLWKAGI 220 A*3201 62 0.63 39 6 143 177 149 159 11 YLHTLWKAGIL 221 B*0801 88 0.85 75 6 143 177 149 159 11 YLHTLWKAGIL 221 B*3901 22 0.85 19 6 143 177 150 159 10 LHTLWKAGIL 222 B*0801 69 0.85 59 6 143 177 150 159 10 LHTLWKAGIL 222 B*3801 51 0.85 43 6 143 177 150 159 10 LHTLWKAGIL 222 B*3901 34 0.85 29 6 143 177 151 159 9 HTLWKAGIL 223 B*5802 1 0.85 1 6 143 177 151 160 10 HTLWKAGILY 224 A*0101 72 1.87 134 6 143 177 151 160 10 HTLWKAGILY 224 A*0301 7 1.87 12 6 143 177 151 160 10 HTLWKAGILY 224 A*2501 47 1.87 88 6 143 177 151 160 10 HTLWKAGILY 224 A*2601 67 1.87 125 6 143 177 151 160 10 HTLWKAGILY 224 A*2902 2 1.87 3 6 143 177 151 160 10 HTLWKAGILY 224 A*3002 49 1.87 92 6 143 177 152 160 9 TLWKAGILY 225 A*0301 36 1.87 67 6 143 177 152 160 9 TLWKAGILY 225 A*2902 78 1.87 145 6 143 177 152 160 9 TLWKAGILY 225 A*3002 4 1.87 8 6 143 177 153 160 8 LWKAGILY 226 A*2902 56 1.87 104 6 143 177 153 160 8 LWKAGILY 226 A*3002 85 1.87 158 6 143 177 153 160 8 LWKAGILY 226 B*3501 8 1.87 15 6 143 177 151 161 11 HTLWKAGILYK 227 A*0301 89 1.41 125 6 143 177 151 161 11 HTLWKAGILYK 227 A*1101 100 1.41 141 6 143 177 151 161 11 HTLWKAGILYK 227 A*3001 78 1.41 110 6 143 177 151 161 11 HTLWKAGILYK 227 A*3101 46 1.41 64 6 143 177 151 161 11 HTLWKAGILYK 227 A*3303 25 1.41 36 6 143 177 151 161 11 HTLWKAGILYK 227 A*6801 75 1.41 106 6 143 177 151 161 11 HTLWKAGILYK 227 A*7401 83 1.41 117 6 143 177 152 161 10 TLWKAGILYK 228 A*0301 87 1.41 122 6 143 177 152 161 10 TLWKAGILYK 228 A*1101 59 1.41 83 6 143 177 152 161 10 TLWKAGILYK 228 A*7401 71 1.41 100 6 143 177 153 161 9 LWKAGILYK 229 A*3001 57 1.41 80 6 143 177 152 162 11 TLWKAGILYKR 230 A*3101 61 1.49 91 6 143 177 152 162 11 TLWKAGILYKR 230 A*3303 72 1.49 107 6 143 177 152 162 11 TLWKAGILYKR 230 A*7401 82 1.49 122 6 143 177 153 162 10 LWKAGILYKR 231 A*3101 86 1.49 128 6 143 177 153 162 10 LWKAGILYKR 231 A*3303 59 1.49 88 6 143 177 155 162 8 KAGILYKR 232 A*3101 67 1.49 100 6 143 177 155 162 8 KAGILYKR 232 A*7401 27 1.49 40 6 143 177 158 166 9 ILYKRETTR 233 A*0301 66 1.75 115 6 143 177 158 166 9 ILYKRETTR 233 A*3101 23 1.75 40 6 143 177 158 166 9 ILYKRETTR 233 A*3303 51 1.75 89 6 143 177 158 166 9 ILYKRETTR 233 A*7401 90 1.75 158 6 143 177 158 168 11 ILYKRETTRSA 234 B*0801 56 1.80 100 6 143 177 160 170 11 YKRETTRSASF 235 B*0702 17 1.82 32 6 143 177 160 170 11 YKRETTRSASF 235 B*0801 81 1.82 148 6 143 177 160 170 11 YKRETTRSASF 235 B*1402 68 1.82 123 6 143 177 160 170 11 YKRETTRSASF 235 B*1501 53 1.82 97 6 143 177 160 170 11 YKRETTRSASF 235 B*1502 65 1.82 118 6 143 177 160 170 11 YKRETTRSASF 235 B*1525 46 1.82 83 6 143 177 161 170 10 KRETTRSASF 236 B*2702 53 1.82 97 6 143 177 162 170 9 RETTRSASF 237 B*4001 57 1.82 103 6 143 177 162 170 9 RETTRSASF 237 B*4402 88 1.82 161 6 143 177 162 170 9 RETTRSASF 237 B*4403 60 1.82 109 6 143 177 162 170 9 RETTRSASF 237 B*5001 44 1.82 80 6 143 177 163 170 8 ETTRSASF 238 A*2501 100 1.82 182 6 143 177 163 170 8 ETTRSASF 238 A*2601 100 1.82 182 6 143 177 166 175 10 RSASFCGSPY 239 A*0101 79 1.16 92 6 143 177 166 175 10 RSASFCGSPY 239 A*2501 45 1.16 52 6 143 177 166 175 10 RSASFCGSPY 239 B*1501 94 1.16 108 6 143 177 166 175 10 RSASFCGSPY 239 B*1502 78 1.16 90 6 143 177 166 175 10 RSASFCGSPY 239 B*1525 80 1.16 92 6 143 177 166 175 10 RSASFCGSPY 239 B*4403 32 1.16 37 6 143 177 166 175 10 RSASFCGSPY 239 B*4601 84 1.16 97 6 143 177 166 175 10 RSASFCGSPY 239 B*5802 68 1.16 79 6 143 177 167 175 9 SASFCGSPY 240 A*3002 79 1.16 91 6 143 177 167 175 9 SASFCGSPY 240 B*3501 81 1.16 94 6 143 177 168 175 8 ASFCGSPY 241 A*1101 70 1.16 80 6 143 177 168 175 8 ASFCGSPY 241 A*2902 54 1.16 62 6 143 177 168 175 8 ASFCGSPY 241 B*5701 44 1.16 51 6 143 177 167 176 10 SASFCGSPYS 242 A*3001 8 0.16 1 6 143 177 167 176 10 SASFCGSPYS 242 B*5701 76 0.16 12 6 143 177 167 176 10 SASFCGSPYS 242 B*5801 76 0.16 12 6 143 177 168 176 9 ASFCGSPYS 243 B*5802 19 0.16 3 6 143 177 167 177 11 SASFCGSPYSW 244 B*5301 79 1.90 150 6 143 177 167 177 11 SASFCGSPYSW 244 B*5701 94 1.90 179 6 143 177 167 177 11 SASFCGSPYSW 244 B*5801 100 1.90 190 6 143 177 167 177 11 SASFCGSPYSW 244 B*5802 100 1.90 190 6 143 177 168 177 10 ASFCGSPYSW 245 B*4402 69 1.90 132 6 143 177 168 177 10 ASFCGSPYSW 245 B*4403 28 1.90 53 6 143 177 168 177 10 ASFCGSPYSW 245 B*5802 99 1.90 188 6 143 177 169 177 9 SFCGSPYSW 246 A*2301 26 1.90 49 6 143 177 Cumulative Class I-BCI score: 10432 137 147 11 DQVVNHYFQTR 191 A*3303 21 1.63 34 7 137 170 138 147 10 QVVNHYFQTR 192 A*3101 1 1.63 2 7 137 170 138 147 10 QVVNHYFQTR 192 A*3303 86 1.63 140 7 137 170 138 147 10 QVVNHYFQTR 192 A*6801 68 1.63 110 7 137 170 138 147 10 QVVNHYFQTR 192 A*7401 17 1.63 28 7 137 170 139 147 9 VVNHYFQTR 193 A*3101 87 1.63 143 7 137 170 139 147 9 VVNHYFQTR 193 A*3303 73 1.63 120 7 137 170 139 147 9 VVNHYFQTR 193 A*7401 72 1.63 117 7 137 170 139 149 11 VVNHYFQTRHY 194 A*0101 42 1.90 79 7 137 170 139 149 11 VVNHYFQTRHY 194 A*2902 70 1.90 133 7 137 170 139 149 11 VVNHYFQTRHY 194 A*3002 90 1.90 172 7 137 170 139 149 11 VVNHYFQTRHY 194 B*1501 50 1.90 95 7 137 170 139 149 11 VVNHYFQTRHY 194 B*1502 44 1.90 85 7 137 170 141 149 9 NHYFQTRHY 195 B*3801 16 1.90 31 7 137 170 142 149 8 HYFQTRHY 196 A*2902 25 1.90 48 7 137 170 142 149 8 HYFQTRHY 196 A*3002 44 1.90 83 7 137 170 141 150 10 NHYFQTRHYL 197 B*1402 94 1.93 181 7 137 170 141 150 10 NHYFQTRHYL 197 B*3801 53 1.93 102 7 137 170 141 150 10 NHYFQTRHYL 197 B*3901 88 1.93 170 7 137 170 142 150 9 HYFQTRHYL 198 A*2301 69 1.93 133 7 137 170 142 150 9 HYFQTRHYL 198 B*1402 34 1.93 66 7 137 170 142 150 9 HYFQTRHYL 198 B*3901 3 1.93 5 7 137 170 143 150 8 YFQTRHYL 199 A*2301 74 1.93 143 7 137 170 143 150 8 YFQTRHYL 199 A*2402 74 1.93 142 7 137 170 143 150 8 YFQTRHYL 199 B*0801 93 1.93 180 7 137 170 142 151 10 HYFQTRHYLH 200 A*2301 33 0.39 13 7 137 170 142 151 10 HYFQTRHYLH 200 A*2402 49 0.39 19 7 137 170 142 151 10 HYFQTRHYLH 200 A*2902 16 0.39 6 7 137 170 143 151 9 YFQTRHYLH 201 A*2902 57 0.39 22 7 137 170 143 153 11 YFQTRHYLHTL 202 A*2301 98 1.22 120 7 137 170 143 153 11 YFQTRHYLHTL 202 A*2402 100 1.22 122 7 137 170 143 153 11 YFQTRHYLHTL 202 B*0801 100 1.22 122 7 137 170 144 153 10 FQTRhYLHTL 203 A*0201 27 1.22 33 7 137 170 144 153 10 FQTRHYLHTL 203 B*1301 63 1.22 77 7 137 170 144 153 10 FQTRHYLHTL 203 B*1402 52 1.22 63 7 137 170 144 153 10 FQTRHYLHTL 203 B*3701 62 1.22 75 7 137 170 144 153 10 FQTRHYLHTL 203 B*3801 71 1.22 87 7 137 170 144 153 10 FQTRHYLHTL 203 B*3901 94 1.22 114 7 137 170 144 153 10 FQTRHYLHTL 203 B*4801 81 1.22 98 7 137 170 145 153 9 QTRHYLHTL 204 A*2501 65 1.22 79 7 137 170 146 153 8 TRHYLHTL 205 B*1402 72 1.22 87 7 137 170 146 153 8 TRHYLHTL 205 B*2702 60 1.22 73 7 137 170 146 153 8 TRHYLHTL 205 B*2705 70 1.22 85 7 137 170 144 154 11 FQTRHYLHTLW 206 B*1301 68 1.50 101 7 137 170 144 154 11 FQTRHYLHTLW 206 B*2702 37 1.50 56 7 137 170 145 154 10 QTRHYLHTLW 207 B*4402 35 1.50 52 7 137 170 145 154 10 QTRHYLHTLW 207 B*5802 70 1.50 104 7 137 170 146 154 9 TRHYLHTLW 208 B*2702 76 1.50 114 7 137 170 147 154 8 RHYLHTLW 209 A*2301 47 1.50 70 7 137 170 147 154 8 RHYLHTLW 209 A*2402 35 1.50 52 7 137 170 147 154 8 RHYLHTLW 209 B*2702 99 1.50 148 7 137 170 147 154 8 RHYLHTLW 209 B*3801 98 1.50 147 7 137 170 147 154 8 RHYLHTLW 209 B*5701 35 1.50 52 7 137 170 147 154 8 RHYLHTLW 209 B*5801 22 1.50 33 7 137 170 147 154 8 RHYLHTLW 209 B*5802 26 1.50 39 7 137 170 145 155 11 QTRHYLHTLWK 210 A*0301 54 0.72 39 7 137 170 145 155 11 QTRHYLHTLWK 210 A*1101 35 0.72 25 7 137 170 145 155 11 QTRHYLHTLWK 210 A*3001 96 0.72 69 7 137 170 146 155 10 TRHYLHTLWK 211 B*2705 36 0.72 26 7 137 170 147 155 9 RHYLHTLWK 212 A*0301 70 0.72 51 7 137 170 147 155 9 RHYLHTLWK 212 B*2702 7 0.72 5 7 137 170 148 155 8 HYLHTLWK 213 A*3101 29 0.72 21 7 137 170 146 156 11 TRHYLHTLWKA 214 B*2705 58 1.23 72 7 137 170 148 156 9 HYLHTLWKA 215 A*2301 31 1.23 38 7 137 170 147 157 11 RHYLHTLWKAG 216 B*2705 6 0.73 4 7 137 170 148 157 10 HYLHTLWKAG 217 A*3201 74 0.73 54 7 137 170 148 158 11 HYLHTLWKAGI 218 A*2301 93 0.63 59 7 137 170 148 158 11 HYLHTLWKAGI 218 A*2402 95 0.63 60 7 137 170 149 158 10 YLHTLWKAGI 219 A*0201 7 0.63 4 7 137 170 151 158 8 HTLWKAGI 220 A*3201 62 0.63 39 7 137 170 149 159 11 YLHTLWKAGIL 221 B*0801 88 0.85 75 7 137 170 149 159 11 YLHTLWKAGIL 221 B*3901 22 0.85 19 7 137 170 150 159 10 LHTLWKAGIL 222 B*0801 69 0.85 59 7 137 170 150 159 10 LHTLWKAGIL 222 B*3801 51 0.85 43 7 137 170 150 159 10 LHTLWKAGIL 222 B*3901 34 0.85 29 7 137 170 151 159 9 HTLWKAGIL 223 B*5802 1 0.85 1 7 137 170 151 160 10 HTLWKAGILY 224 A*0101 72 1.87 134 7 137 170 151 160 10 HTLWKAGILY 224 A*0301 7 1.87 12 7 137 170 151 160 10 HTLWKAGILY 224 A*2501 47 1.87 88 7 137 170 151 160 10 HTLWKAGILY 224 A*2601 67 1.87 125 7 137 170 151 160 10 HTLWKAGILY 224 A*2902 2 1.87 3 7 137 170 151 160 10 HTLWKAGILY 224 A*3002 49 1.87 92 7 137 170 152 160 9 TLWKAGILY 225 A*0301 36 1.87 67 7 137 170 152 160 9 TLWKAGILY 225 A*2902 78 1.87 145 7 137 170 152 160 9 TLWKAGILY 225 A*3002 4 1.87 8 7 137 170 153 160 8 LWKAGILY 226 A*2902 56 1.87 104 7 137 170 153 160 8 LWKAGILY 226 A*3002 85 1.87 158 7 137 170 153 160 8 LWKAGILY 226 B*3501 8 1.87 15 7 137 170 151 161 11 HTLWKAGILYK 227 A*0301 89 1.41 125 7 137 170 151 161 11 HTLWKAGILYK 227 A*1101 100 1.41 141 7 137 170 151 161 11 HTLWKAGILYK 227 A*3001 78 1.41 110 7 137 170 151 161 11 HTLWKAGILYK 227 A*3101 46 1.41 64 7 137 170 151 161 11 HTLWKAGILYK 227 A*3303 25 1.41 36 7 137 170 151 161 11 HTLWKAGILYK 227 A*6801 75 1.41 106 7 137 170 151 161 11 HTLWKAGILYK 227 A*7401 83 1.41 117 7 137 170 152 161 10 TLWKAGILYK 228 A*0301 87 1.41 122 7 137 170 152 161 10 TLWKAGILYK 228 A*1101 59 1.41 83 7 137 170 152 161 10 TLWKAGILYK 228 A*7401 71 1.41 100 7 137 170 153 161 9 LWKAGILYK 229 A*3001 57 1.41 80 7 137 170 152 162 11 TLWKAGILYKR 230 A*3101 61 1.49 91 7 137 170 152 162 11 TLWKAGILYKR 230 A*3303 72 1.49 107 7 137 170 152 162 11 TLWKAGILYKR 230 A*7401 82 1.49 122 7 137 170 153 162 10 LWKAGILYKR 231 A*3101 86 1.49 128 7 137 170 153 162 10 LWKAGILYKR 231 A*3303 59 1.49 88 7 137 170 155 162 8 KAGILYKR 232 A*3101 67 1.49 100 7 137 170 155 162 8 KAGILYKR 232 A*7401 27 1.49 40 7 137 170 158 166 9 ILYKRETTR 233 A*0301 66 1.75 115 7 137 170 158 166 9 ILYKRETTR 233 A*3101 23 1.75 40 7 137 170 158 166 9 ILYKRETTR 233 A*3303 51 1.75 89 7 137 170 158 166 9 ILYKRETTR 233 A*7401 90 1.75 158 7 137 170 158 168 11 ILYKRETTRSA 234 B*0801 56 1.80 100 7 137 170 160 170 11 YKRETTRSASF 235 B*0702 17 1.82 32 7 137 170 160 170 11 YKRETTRSASF 235 B*0801 81 1.82 148 7 137 170 160 170 11 YKRETTRSASF 235 B*1402 68 1.82 123 7 137 170 160 170 11 YKRETTRSASF 235 B*1501 53 1.82 97 7 137 170 160 170 11 YKRETTRSASF 235 B*1502 65 1.82 118 7 137 170 160 170 11 YKRETTRSASF 235 B*1525 46 1.82 83 7 137 170 161 170 10 KRETTRSASF 236 B*2702 53 1.82 97 7 137 170 162 170 9 RETTRSASF 237 B*4001 57 1.82 103 7 137 170 162 170 9 RETTRSASF 237 B*4402 88 1.82 161 7 137 170 162 170 9 RETTRSASF 237 B*4403 60 1.82 109 7 137 170 162 170 9 RETTRSASF 237 B*5001 44 1.82 80 7 137 170 163 170 8 ETTRSASF 238 A*2501 100 1.82 182 7 137 170 163 170 8 ETTRSASF 238 A*2601 100 1.82 182 7 137 170 Cumulative Class I-BCI score: 10325 316 326 11 SQSQGSVSSCW 247 B*4402 46 1.49 69 8 316 347 316 326 11 SQSQGSVSSCW 247 B*4403 24 1.49 36 8 316 347 317 326 10 QSQGSVSSCW 248 B*4402 54 1.49 80 8 316 347 317 326 10 QSQGSVSSCW 248 B*5802 64 1.49 95 8 316 347 319 326 8 QGSYSSCW 249 B*5801 15 1.49 23 8 316 347 317 327 11 QSQGSVSSCWW 250 B*5701 79 1.02 80 8 316 347 317 327 11 QSQGSVSSCWW 250 B*5801 88 1.02 90 8 316 347 317 327 11 QSQGSVSSCWW 250 B*5802 75 1.02 77 8 316 347 319 327 9 QGSYSSCWW 251 B*5701 38 1.02 39 8 316 347 319 327 9 QGSYSSCWW 251 B*5801 10 1.02 10 8 316 347 320 327 8 GSYSSCWW 252 B*5701 92 1.02 94 8 316 347 320 327 8 GSYSSCWW 252 B*5801 95 1.02 97 8 316 347 320 327 8 GSYSSCWW 252 B*5802 84 1.02 86 8 316 347 318 328 11 SQGSVSSCWWL 253 B*4801 37 1.77 65 8 316 347 320 329 10 GSVSSCWWLQ 254 A*3201 21 0.81 17 8 316 347 320 330 11 GSVSSCWWLQF 255 B*1525 22 1.91 42 8 316 347 320 330 11 GSVSSCWWLQF 255 B*5701 74 1.91 142 8 316 347 320 330 11 GSVSSCWWLQF 255 B*5802 65 1.91 125 8 316 347 321 330 10 SVSSCWWLQF 256 A*2601 31 1.91 59 8 316 347 321 330 10 SVSSCWWLQF 256 A*3201 58 1.91 110 8 316 347 322 330 9 VSSCWWLQF 257 A*0101 53 1.91 101 8 316 347 322 330 9 VSSCWWLQF 257 A*2402 23 1.91 44 8 316 347 322 330 9 VSSCWWLQF 257 B*4601 21 1.91 41 8 316 347 322 330 9 VSSCWWLQF 257 B*5701 58 1.91 110 8 316 347 322 330 9 VSSCWWLQF 257 B*5801 73 1.91 139 8 316 347 323 330 8 SSCWWLQF 258 A*2301 21 1.91 40 8 316 347 323 330 8 SSCWWLQF 258 A*3201 42 1.91 81 8 316 347 323 330 8 SSCWWLQF 258 B*5801 59 1.91 113 8 316 347 321 331 11 SVSSCWWLQFR 259 A*1101 65 0.81 53 8 316 347 321 331 11 SVSSCWWLQFR 259 A*3303 100 0.81 81 8 316 347 321 331 11 SVSSCWWLQFR 259 A*6801 96 0.81 78 8 316 347 321 331 11 SVSSCWWLQFR 259 A*7401 98 0.81 79 8 316 347 322 331 10 VSSCWWLQFR 260 A*3101 95 0.81 77 8 316 347 322 331 10 VSSCWWLQFR 260 A*3303 56 0.81 46 8 316 347 322 331 10 VSSCWWLQFR 260 B*5701 30 0.81 25 8 316 347 322 331 10 VSSCWWLQFR 260 B*5801 42 0.81 34 8 316 347 323 331 9 SSCWWLQFR 261 A*1101 41 0.81 34 8 316 347 323 331 9 SSCWWLQFR 261 A*3101 94 0.81 76 8 316 347 323 331 9 SSCWWLQFR 261 A*3303 85 0.81 69 8 316 347 323 331 9 SSCWWLQFR 261 A*7401 87 0.81 70 8 316 347 324 331 8 SCWWLQFR 262 A*3303 44 0.81 36 8 316 347 327 334 8 WLQFRNSK 263 A*0301 20 0.52 10 8 316 347 328 335 8 LQFRNSKP 264 A*0206 21 0.10 2 8 316 347 327 336 10 WLQFrNSKPC 265 A*0201 18 0.14 3 8 316 347 328 337 10 LQFRNSKPCS 266 A*3001 99 0.26 26 8 316 347 329 339 11 QFRNSKPCSEY 267 A*3002 10 1.63 16 8 316 347 331 339 9 RNSKPCSEY 268 A*3002 8 1.63 14 8 316 347 332 339 8 NSKPCSEY 269 A*3002 20 1.63 32 8 316 347 336 343 8 CSEYCLSH 270 A*0101 40 0.58 23 8 316 347 337 344 8 SEYCLSHL 271 B*1301 97 1.01 98 8 316 347 337 344 8 SEYCLSHL 271 B*1302 37 1.01 37 8 316 347 337 344 8 SEYCLSHL 271 B*1801 67 1.01 67 8 316 347 337 344 8 SEYCLSHL 271 B*3701 100 1.01 101 8 316 347 337 344 8 SEYCLSHL 271 B*3801 96 1.01 97 8 316 347 337 344 8 SEYCLSHL 271 B*4001 100 1.01 101 8 316 347 337 344 8 SEYCLSHL 271 B*4002 100 1.01 101 8 316 347 337 344 8 SEYCLSHL 271 B*4402 85 1.01 85 8 316 347 337 344 8 SEYCLSHL 271 B*4403 88 1.01 89 8 316 347 337 344 8 SEYCLSHL 271 B*4801 46 1.01 47 8 316 347 337 344 8 SEYCLSHL 271 B*4901 96 1.01 97 8 316 347 337 344 8 SEYCLSHL 271 B*5001 96 1.01 97 8 316 347 337 344 8 SEYCLSHL 271 B*5201 57 1.01 57 8 316 347 335 345 11 PCSEYCLSHLV 272 A*0201 40 1.78 71 8 316 347 337 345 9 SEYCLSHLV 273 B*1301 94 1.78 168 8 316 347 337 345 9 SEYCLSHLV 273 B*1302 48 1.78 85 8 316 347 337 345 9 SEYCLSHLV 273 B*1801 29 1.78 51 8 316 347 337 345 9 SEYCLSHLV 273 B*4001 65 1.78 116 8 316 347 337 345 9 SEYCLSHLV 273 B*4002 70 1.78 125 8 316 347 337 345 9 SEYCLSHLV 273 B*4402 77 1.78 137 8 316 347 337 345 9 SEYCLSHLV 273 B*4403 80 1.78 142 8 316 347 337 345 9 SEYCLSHLV 273 B*4901 100 1.78 178 8 316 347 337 345 9 SEYCLSHLV 273 B*5001 100 1.78 178 8 316 347 337 345 9 SEYCLSHLV 273 B*5201 71 1.78 126 8 316 347 337 346 10 SEYCLSHLVN 274 B*4001 39 0.24 10 8 316 347 337 346 10 SEYCLSHLVN 274 B*4403 76 0.24 18 8 316 347 337 346 10 SEYCLSHLVN 274 B*5001 24 0.24 6 8 316 347 337 347 11 SEYCLSHLVNL 275 B*1301 100 1.66 166 8 316 347 337 347 11 SEYCLSHLVNL 275 B*1302 45 1.66 75 8 316 347 337 347 11 SEYCLSHLVNL 275 B*1801 86 1.66 142 8 316 347 337 347 11 SEYCLSHLVNL 275 B*3701 95 1.66 158 8 316 347 337 347 11 SEYCLSHLVNL 275 B*3801 94 1.66 156 8 316 347 337 347 11 SEYCLSHLVNL 275 B*4001 96 1.66 158 8 316 347 337 347 11 SEYCLSHLVNL 275 B*4002 95 1.66 157 8 316 347 337 347 11 SEYCLSHLVNL 275 B*4402 81 1.66 134 8 316 347 337 347 11 SEYCLSHLVNL 275 B*4403 84 1.66 139 8 316 347 337 347 11 SEYCLSHLVNL 275 B*4901 91 1.66 151 8 316 347 337 347 11 SEYCLSHLVNL 275 B*5001 92 1.66 152 8 316 347 337 347 11 SEYCLSHLVNL 275 B*5201 63 1.66 104 8 316 347 338 347 10 EYCLSHLVNL 276 A*2301 48 1.66 80 8 316 347 Cumulative Class I-BCI score: 7246 386 394 9 AESRLVVDF 278 B*1801 10 1.80 17 9 385 417 386 394 9 AESRLVVDF 278 B*4001 48 1.80 86 9 385 417 386 394 9 AESRLVVDF 278 B*4002 50 1.80 90 9 385 417 386 394 9 AESRLVVDF 278 B*4402 100 1.80 180 9 385 417 386 394 9 AESRLVVDF 278 B*4403 100 1.80 180 9 385 417 386 394 9 AESRLVVDF 278 B*4901 43 1.80 78 9 385 417 386 394 9 AESRLVVDF 278 B*5001 36 1.80 65 9 385 417 386 396 11 AESRLVVDFSQ 279 B*4402 15 0.65 10 9 385 417 386 396 11 AESRLVVDFSQ 279 B*4403 8 0.65 5 9 385 417 387 397 11 ESRLVVDFSQF 280 A*2501 49 1.86 91 9 385 417 387 397 11 ESRLVVDFSQF 280 A*2601 5 1.86 10 9 385 417 388 397 10 SRLVVDFSQF 281 B*2702 92 1.86 170 9 385 417 389 397 9 RLVVDFSQF 282 A*2301 43 1.86 80 9 385 417 389 397 9 RLVVDFSQF 282 B*1501 70 1.86 131 9 385 417 389 397 9 RLVVDFSQF 282 B*1525 78 1.86 145 9 385 417 390 397 8 LVVDFSQF 283 A*2501 59 1.86 110 9 385 417 390 397 8 LVVDFSQF 283 A*2601 79 1.86 148 9 385 417 390 397 8 LVVDFSQF 283 B*1501 59 1.86 110 9 385 417 390 397 8 LVVDFSQF 283 B*1502 72 1.86 134 9 385 417 390 397 8 LVVDFSQF 283 B*1525 56 1.86 104 9 385 417 390 397 8 LVVDFSQF 283 B*4601 57 1.86 107 9 385 417 389 399 11 RLVVDFSQFSR 284 A*0301 15 1.78 26 9 385 417 389 399 11 RLVVDFSQFSR 284 A*3101 81 1.78 144 9 385 417 389 399 11 RLVVDFSQFSR 284 A*7401 96 1.78 172 9 385 417 390 399 10 LVVDFSQFSR 285 A*3101 89 1.78 158 9 385 417 390 399 10 LVVDFSQFSR 285 A*3201 6 1.78 11 9 385 417 390 399 10 LVVDFSQFSR 285 A*3303 83 1.78 148 9 385 417 390 399 10 LVVDFSQFSR 285 A*6801 88 1.78 157 9 385 417 390 399 10 LVVDFSQFSR 285 A*7401 70 1.78 124 9 385 417 391 399 9 VVDFSQFSR 286 A*1101 11 1.78 19 9 385 417 391 399 9 VVDFSQFSR 286 A*3303 18 1.78 33 9 385 417 391 399 9 VVDFSQFSR 286 A*7401 79 1.78 141 9 385 417 390 400 11 LVVDFSQFSRG 287 A*6802 6 0.16 1 9 385 417 392 401 10 VDFSQFSRGI 288 B*1301 76 1.23 93 9 385 417 392 401 10 VDFSQFSRGI 288 B*1302 44 1.23 54 9 385 417 392 401 10 VDFSQFSRGI 288 B*5201 88 1.23 108 9 385 417 393 403 11 DFSQFSRGISR 289 A*3303 55 0.77 42 9 385 417 394 403 10 FSQFSRGISR 290 A*3101 14 0.77 11 9 385 417 394 403 10 FSQFSRGISR 290 A*3303 11 0.77 9 9 385 417 394 403 10 FSQFSRGISR 290 A*6801 60 0.77 46 9 385 417 395 403 9 SQFSRGISR 291 A*1101 13 0.77 10 9 385 417 395 403 9 SQFSRGISR 291 A*3101 62 0.77 48 9 385 417 395 403 9 SQFSRGISR 291 A*3303 70 0.77 54 9 385 417 395 403 9 SQFSRGISR 291 A*7401 95 0.77 73 9 385 417 396 403 8 QFSRGISR 292 A*3303 48 0.77 37 9 385 417 395 404 10 SQFSrGISRV 293 A*0201 45 1.90 85 9 385 417 395 404 10 SQFSRGISRV 293 B*1302 23 1.90 43 9 385 417 395 404 10 SQFSRGISRV 293 B*1402 4 1.90 8 9 385 417 395 404 10 SQFSRGISRV 293 B*3901 27 1.90 52 9 385 417 395 404 10 SQFSRGISRV 293 B*4801 35 1.90 66 9 385 417 395 404 10 SQFSRGISRV 293 B*5201 69 1.90 130 9 385 417 398 405 8 SRGISRVS 294 B*2705 12 0.22 3 9 385 417 397 406 10 FSRGISRVSW 295 B*4601 38 1.40 53 9 385 417 397 406 10 FSRGISRVSW 295 B*5301 15 1.40 21 9 385 417 397 406 10 FSRGISRVSW 295 B*5802 87 1.40 122 9 385 417 398 406 9 SRGISRVSW 296 B*2702 65 1.40 91 9 385 417 399 406 8 RGISRVSW 297 B*2702 28 1.40 39 9 385 417 399 406 8 RGISRVSW 297 B*5701 73 1.40 102 9 385 417 399 406 8 RGISRVSW 297 B*5801 68 1.40 95 9 385 417 399 406 8 RGISRVSW 297 B*5802 74 1.40 103 9 385 417 400 408 9 GISRVSWPK 298 A*0301 62 0.98 61 9 385 417 400 408 9 GISRVSWPK 298 A*1101 93 0.98 91 9 385 417 400 408 9 GISRVSWPK 298 A*7401 40 0.98 39 9 385 417 401 408 8 ISRVSWPK 299 A*0301 13 0.98 13 9 385 417 401 408 8 ISRVSWPK 299 A*1101 30 0.98 30 9 385 417 401 408 8 ISRVSWPK 299 A*3001 95 0.98 92 9 385 417 399 409 11 RGISRVSWPKF 300 A*2301 7 1.38 10 9 385 417 399 409 11 RGISRVSWPKF 300 B*5802 7 1.38 10 9 385 417 400 409 10 GISRVSWPKF 301 A*3001 55 1.38 77 9 385 417 400 409 10 GISRVSWPKF 301 A*3201 98 1.38 136 9 385 417 401 409 9 ISRVSWPKF 302 B*5701 88 1.38 122 9 385 417 402 409 8 SRVSWPKF 303 B*2702 90 1.38 125 9 385 417 402 409 8 SRVSWPKF 303 B*2705 57 1.38 78 9 385 417 403 410 8 RVSWPKFA 304 A*3001 16 0.84 14 9 385 417 401 411 11 ISRVSWPKFAV 305 A*3001 70 1.60 111 9 385 417 402 411 10 SRVSWPKFAV 306 B*3901 6 1.60 10 9 385 417 403 411 9 RVSWPKFAV 307 A*6802 4 1.60 7 9 385 417 403 411 9 RVSWPKFAV 307 B*0702 6 1.60 9 9 385 417 404 411 8 VSWPKFAV 308 B*5201 41 1.60 66 9 385 417 405 412 8 SWPKFAVP 309 A*0206 100 0.48 48 9 385 417 404 414 11 VSWPKFAVPNL 310 B*5201 16 1.63 26 9 385 417 404 414 11 VSWPKFAVPNL 310 B*5701 18 1.63 30 9 385 417 405 414 10 SWPKFAVPNL 311 A*2301 78 1.63 127 9 385 417 405 414 10 SWPKFAVPNL 311 A*2402 75 1.63 123 9 385 417 406 414 9 WPKFAVPNL 312 B*1402 21 1.63 35 9 385 417 406 414 9 WPKFAVPNL 312 B*3503 18 1.63 29 9 385 417 409 417 9 FAVPNLQSL 313 A*0206 54 1.89 102 9 385 417 409 417 9 FAVPNLQSL 313 B*3503 46 1.89 87 9 385 417 409 417 9 FAVPNLQSL 313 B*4601 95 1.89 180 9 385 417 410 417 8 AVPNLQSL 314 B*0702 29 1.89 55 9 385 417 Cumulative BCI Class I score: 6722 420 427 8 LLSSNLSW 316 B*5301 20 1.77 35 10 419 456 420 427 8 LLSSNLSW 316 B*5701 48 1.77 86 10 419 456 420 427 8 LLSSNLSW 316 B*5801 66 1.77 117 10 419 456 420 427 8 LLSSNLSW 316 B*5802 30 1.77 54 10 419 456 419 428 10 NLLSsNLSWL 317 A*0201 100 1.54 154 10 419 456 420 428 9 LLSSNLSWL 318 A*0201 86 1.54 133 10 419 456 421 428 8 LSSNLSWL 319 B*0702 78 1.54 121 10 419 456 421 429 9 LSSNLSWLS 320 A*0101 30 0.55 16 10 419 456 420 430 11 LLSSNLSWLSL 321 B*0801 8 1.74 15 10 419 456 421 430 10 LSSNLSWLSL 322 A*3201 47 1.74 82 10 419 456 421 430 10 LSSNLSWLSL 322 B*5701 27 1.74 48 10 419 456 421 430 10 LSSNLSWLSL 322 B*5801 3 1.74 6 10 419 456 421 430 10 LSSNLSWLSL 322 B*5802 29 1.74 50 10 419 456 422 431 10 SSNLSWLSLD 323 A*3001 22 0.11 2 10 419 456 422 432 11 SSNLSWLSLDV 324 A*0201 38 1.41 53 10 419 456 424 432 9 NLSWLSLDV 325 A*0201 29 1.41 41 10 419 456 425 432 8 LSWLSLDV 326 A*0206 4 1.41 6 10 419 456 425 432 8 LSWLSLDV 326 B*1302 1 1.41 2 10 419 456 425 432 8 LSWLSLDV 326 B*5201 55 1.41 77 10 419 456 425 435 11 LSWLSLDVSAA 327 B*5601 9 0.74 7 10 419 456 427 435 9 WLSLDVSAA 328 A*0201 14 0.74 10 10 419 456 426 436 11 SWLSLDVSAAF 329 A*2301 91 1.90 174 10 419 456 426 436 11 SWLSLDVSAAF 329 A*2402 93 1.90 177 10 419 456 426 436 11 SWLSLDVSAAF 329 A*2902 32 1.90 60 10 419 456 426 436 11 SWLSLDVSAAF 329 B*1801 38 1.90 72 10 419 456 427 436 10 WLSLDVSAAF 330 B*1501 72 1.90 137 10 419 456 427 436 10 WLSLDVSAAF 330 B*1502 89 1.90 169 10 419 456 427 436 10 WLSLDVSAAF 330 B*1525 54 1.90 103 10 419 456 428 436 9 LSLDVSAAF 331 B*1501 73 1.90 140 10 419 456 428 436 9 LSLDVSAAF 331 B*1525 76 1.90 145 10 419 456 428 436 9 LSLDVSAAF 331 B*3501 69 1.90 132 10 419 456 428 436 9 LSLDVSAAF 331 B*3503 51 1.90 98 10 419 456 428 436 9 LSLDVSAAF 331 B*4601 75 1.90 144 10 419 456 428 436 9 LSLDVSAAF 331 B*5801 63 1.90 119 10 419 456 427 437 11 WLSLDVSAAFY 332 A*0101 74 1.81 133 10 419 456 427 437 11 WLSLDVSAAFY 332 A*2601 38 1.81 69 10 419 456 427 437 11 WLSLDVSAAFY 332 A*2902 75 1.81 135 10 419 456 427 437 11 WLSLDVSAAFY 332 B*1502 22 1.81 40 10 419 456 428 437 10 LSLDVSAAFY 333 A*0101 100 1.81 181 10 419 456 428 437 10 LSLDVSAAFY 333 A*2902 83 1.81 149 10 419 456 428 437 10 LSLDVSAAFY 333 A*3002 99 1.81 178 10 419 456 428 437 10 LSLDVSAAFY 333 B*1501 22 1.81 40 10 419 456 428 437 10 LSLDVSAAFY 333 B*4601 69 1.81 124 10 419 456 428 437 10 LSLDVSAAFY 333 B*5802 57 1.81 102 10 419 456 429 437 9 SLDVSAAFY 334 A*0101 85 1.81 153 10 419 456 429 437 9 SLDVSAAFY 334 A*3002 59 1.81 107 10 419 456 430 437 8 LDVSAAFY 335 B*3501 31 1.81 55 10 419 456 430 439 10 LDVSAAFYHI 336 B*1301 96 1.79 171 10 419 456 430 439 10 LDVSAAFYHI 336 B*1302 49 1.79 88 10 419 456 430 439 10 LDVSAAFYHI 336 B*3701 57 1.79 102 10 419 456 430 439 10 LDVSAAFYHI 336 B*4901 57 1.79 101 10 419 456 430 439 10 LDVSAAFYHI 336 B*5201 98 1.79 175 10 419 456 431 439 9 DVSAAFYHI 337 A*6802 46 1.79 81 10 419 456 432 439 8 VSAAFYHI 338 A*3201 18 1.79 32 10 419 456 432 439 8 VSAAFYHI 338 B*1302 28 1.79 50 10 419 456 432 439 8 VSAAFYHI 338 B*5101 8 1.79 15 10 419 456 432 439 8 VSAAFYHI 338 B*5201 96 1.79 172 10 419 456 432 439 8 VSAAFYHI 338 B*5701 65 1.79 116 10 419 456 432 439 8 VSAAFYHI 338 B*5801 64 1.79 115 10 419 456 432 439 8 VSAAFYHI 338 B*5802 49 1.79 88 10 419 456 431 441 11 DVSAAFYHIPL 339 A*2501 33 1.00 33 10 419 456 431 441 11 DVSAAFYHIPL 339 A*2601 51 1.00 51 10 419 456 432 441 10 VSAAFYHIPL 340 A*6802 35 1.00 35 10 419 456 432 441 10 VSAAFYHIPL 340 B*5802 14 1.00 15 10 419 456 433 441 9 SAAFYHIPL 341 B*1402 79 1.00 79 10 419 456 433 441 9 SAAFYHIPL 341 B*3503 34 1.00 34 10 419 456 434 441 8 AAFYHIPL 342 B*0801 64 1.00 65 10 419 456 434 441 8 AAFYHIPL 342 B*1402 57 1.00 57 10 419 456 434 441 8 AAFYHIPL 342 B*3801 6 1.00 6 10 419 456 434 441 8 AAFYHIPL 342 B*3901 32 1.00 33 10 419 456 434 441 8 AAFYHIPL 342 B*4801 63 1.00 64 10 419 456 433 442 10 SAAFYHIPLH 343 A*3001 83 0.25 20 10 419 456 434 444 11 AAFYHIPLHPA 344 A*3001 11 0.89 10 10 419 456 434 444 11 AAFYHIPLHPA 344 B*5501 20 0.89 18 10 419 456 434 444 11 AAFYHIPLHPA 344 B*5601 21 0.89 18 10 419 456 437 444 8 YHIPLHPA 345 B*1402 19 0.89 17 10 419 456 437 444 8 YHIPLHPA 345 B*3901 87 0.89 78 10 419 456 437 445 9 YHIPLHPAA 346 B*1402 18 0.62 11 10 419 456 436 446 11 FYHIPLHPAAM 347 A*2402 19 1.63 31 10 419 456 437 446 10 YHIPLHPAAM 348 B*1402 99 1.63 161 10 419 456 437 446 10 YHIPLHPAAM 348 B*3503 74 1.63 121 10 419 456 437 446 10 YHIPLHPAAM 348 B*3801 86 1.63 140 10 419 456 437 446 10 YHIPLHPAAM 348 B*3901 100 1.63 163 10 419 456 438 446 9 HIPLHPAAM 349 A*2501 73 1.63 120 10 419 456 438 446 9 HIPLHPAAM 349 B*1402 3 1.63 5 10 419 456 439 446 8 IPLHPAAM 350 B*1402 86 1.63 140 10 419 456 439 446 8 IPLHPAAM 350 B*3503 93 1.63 152 10 419 456 439 446 8 IPLHPAAM 350 B*5101 55 1.63 90 10 419 456 439 446 8 IPLHPAAM 350 B*5301 64 1.63 104 10 419 456 439 446 8 IPLHPAAM 350 B*5501 85 1.63 138 10 419 456 439 446 8 IPLHPAAM 350 B*5601 73 1.63 119 10 419 456 439 449 11 IPLHPAAMPHL 351 B*0702 58 1.61 93 10 419 456 439 449 11 IPLHPAAMPHL 351 B*1402 31 1.61 50 10 419 456 439 449 11 IPLHPAAMPHL 351 B*3503 32 1.61 52 10 419 456 439 449 11 IPLHPAAMPHL 351 B*5101 53 1.61 86 10 419 456 439 449 11 IPLHPAAMPHL 351 B*5501 38 1.61 62 10 419 456 441 449 9 LHPAAMPHL 352 B*3801 76 1.61 121 10 419 456 442 449 8 HPAAMPHL 353 B*1402 85 1.61 136 10 419 456 442 449 8 HPAAMPHL 353 B*3503 73 1.61 117 10 419 456 442 449 8 HPAAMPHL 353 B*3901 53 1.61 85 10 419 456 442 449 8 HPAAMPHL 353 B*5101 48 1.61 78 10 419 456 442 449 8 HPAAMPHL 353 B*5301 38 1.61 61 10 419 456 442 449 8 HPAAMPHL 353 B*5501 55 1.61 88 10 419 456 442 449 8 HPAAMPHL 353 B*5601 29 1.61 47 10 419 456 441 450 10 LHPAAMPHLL 354 B*3801 67 1.81 122 10 419 456 442 450 9 HPAAMPHLL 355 B*0702 70 1.81 126 10 419 456 442 450 9 HPAAMPHLL 355 B*1402 93 1.81 168 10 419 456 442 450 9 HPAAMPHLL 355 B*3501 29 1.81 53 10 419 456 442 450 9 HPAAMPHLL 355 B*3503 85 1.81 154 10 419 456 442 450 9 HPAAMPHLL 355 B*3901 97 1.81 176 10 419 456 442 450 9 HPAAMPHLL 355 B*5301 33 1.81 59 10 419 456 442 450 9 HPAAMPHLL 355 B*5501 72 1.81 130 10 419 456 442 450 9 HPAAMPHLL 355 B*5601 58 1.81 104 10 419 456 441 451 11 LHPAAMPHLLI 356 B*3801 61 0.84 51 10 419 456 442 451 10 HPAAMPHLLI 357 B*1402 71 0.84 59 10 419 456 442 451 10 HPAAMPHLLI 357 B*3503 72 0.84 60 10 419 456 442 451 10 HPAAMPHLLI 357 B*3901 38 0.84 31 10 419 456 442 451 10 HPAAMPHLLI 357 B*5201 61 0.84 51 10 419 456 442 451 10 HPAAMPHLLI 357 B*5301 36 0.84 30 10 419 456 442 451 10 HPAAMPHLLI 357 B*5501 84 0.84 70 10 419 456 442 451 10 HPAAMPHLLI 357 B*5601 90 0.84 75 10 419 456 444 451 8 AAMPHLLI 358 A*3201 59 0.84 49 10 419 456 444 451 8 AAMPHLLI 358 B*1302 35 0.84 29 10 419 456 444 451 8 AAMPHLLI 358 B*5101 47 0.84 39 10 419 456 444 451 8 AAMPHLLI 358 B*5201 94 0.84 79 10 419 456 444 451 8 AAMPHLLI 358 B*5801 37 0.84 31 10 419 456 442 452 11 HPAAMPHLLIG 359 A*0201 51 0.32 16 10 419 456 442 452 11 HPAAMPHLLIG 359 A*0206 38 0.32 12 10 419 456 446 453 8 MPHLLIGS 360 A*6802 16 0.77 12 10 419 456 446 453 8 MPHLLIGS 360 B*5601 28 0.77 22 10 419 456 446 454 9 MPHLLIGSS 361 B*5501 37 0.26 10 10 419 456 446 454 9 MPHLLIGSS 361 B*5601 41 0.26 11 10 419 456 446 455 10 MPHLLIGSSG 362 B*0702 35 0.11 4 10 419 456 446 455 10 MPHLLIGSSG 362 B*3501 40 0.11 4 10 419 456 446 455 10 MPHLLIGSSG 362 B*5501 3 0.11 0 10 419 456 446 455 10 MPHLLIGSSG 362 B*5601 18 0.11 2 10 419 456 446 456 11 MPHLLIGSSGL 363 B*0702 93 1.81 168 10 419 456 446 456 11 MPHLLIGSSGL 363 B*0801 44 1.81 80 10 419 456 446 456 11 MPHLLIGSSGL 363 B*1402 92 1.81 167 10 419 456 446 456 11 MPHLLIGSSGL 363 B*3501 27 1.81 48 10 419 456 446 456 11 MPHLLIGSSGL 363 B*3503 70 1.81 127 10 419 456 446 456 11 MPHLLIGSSGL 363 B*3901 62 1.81 113 10 419 456 446 456 11 MPHLLIGSSGL 363 B*5101 40 1.81 73 10 419 456 446 456 11 MPHLLIGSSGL 363 B*5301 18 1.81 33 10 419 456 446 456 11 MPHLLIGSSGL 363 B*5501 71 1.81 129 10 419 456 446 456 11 MPHLLIGSSGL 363 B*5601 53 1.81 95 10 419 456 448 456 9 HLLIGSSGL 364 B*1502 83 1.81 151 10 419 456 449 456 8 LLIGSSGL 365 B*0702 77 1.81 139 10 419 456 Cumulative BCI Class Iscore: 11926 422 432 11 SSNLSWLSLDV 324 A*0201 38 1.41 53 11 422 459 424 432 9 NLSWLSLDV 325 A*0201 29 1.41 41 11 422 459 425 432 8 LSWLSLDV 326 A*0206 4 1.41 6 11 422 459 425 432 8 LSWLSLDV 326 B*1302 1 1.41 2 11 422 459 425 432 8 LSWLSLDV 326 B*5201 55 1.41 77 11 422 459 425 435 11 LSWLSLDVSAA 327 B*5601 9 0.74 7 11 422 459 427 435 9 WLSLDVSAA 328 A*0201 14 0.74 10 11 422 459 426 436 11 SWLSLDVSAAF 329 A*2301 91 1.90 174 11 422 459 426 436 11 SWLSLDVSAAF 329 A*2402 93 1.90 177 11 422 459 426 436 11 SWLSLDVSAAF 329 A*2902 32 1.90 60 11 422 459 426 436 11 SWLSLDVSAAF 329 B*1801 38 1.90 72 11 422 459 427 436 10 WLSLDVSAAF 330 B*1501 72 1.90 137 11 422 459 427 436 10 WLSLDVSAAF 330 B*1502 89 1.90 169 11 422 459 427 436 10 WLSLDVSAAF 330 B*1525 54 1.90 103 11 422 459 428 436 9 LSLDVSAAF 331 B*1501 73 1.90 140 11 422 459 428 436 9 LSLDVSAAF 331 B*1525 76 1.90 145 11 422 459 428 436 9 LSLDVSAAF 331 B*3501 69 1.90 132 11 422 459 428 436 9 LSLDVSAAF 331 B*3503 51 1.90 98 11 422 459 428 436 9 LSLDVSAAF 331 B*4601 75 1.90 144 11 422 459 428 436 9 LSLDVSAAF 331 B*5801 63 1.90 119 11 422 459 427 437 11 WLSLDVSAAFY 332 A*0101 74 1.81 133 11 422 459 427 437 11 WLSLDVSAAFY 332 A*2601 38 1.81 69 11 422 459 427 437 11 WLSLDVSAAFY 332 A*2902 75 1.81 135 11 422 459 427 437 11 WLSLDVSAAFY 332 B*1502 22 1.81 40 11 422 459 428 437 10 LSLDVSAAFY 333 A*0101 100 1.81 181 11 422 459 428 437 10 LSLDVSAAFY 333 A*2902 83 1.81 149 11 422 459 428 437 10 LSLDVSAAFY 333 A*3002 99 1.81 178 11 422 459 428 437 10 LSLDVSAAFY 333 B*1501 22 1.81 40 11 422 459 428 437 10 LSLDVSAAFY 333 B*4601 69 1.81 124 11 422 459 428 437 10 LSLDVSAAFY 333 B*5802 57 1.81 102 11 422 459 429 437 9 SLDVSAAFY 334 A*0101 85 1.81 153 11 422 459 429 437 9 SLDVSAAFY 334 A*3002 59 1.81 107 11 422 459 430 437 8 LDVSAAFY 335 B*3501 31 1.81 55 11 422 459 430 439 10 LDVSAAFYHI 336 B*1301 96 1.79 171 11 422 459 430 439 10 LDVSAAFYHI 336 B*1302 49 1.79 88 11 422 459 430 439 10 LDVSAAFYHI 336 B*3701 57 1.79 102 11 422 459 430 439 10 LDVSAAFYHI 336 B*4901 57 1.79 101 11 422 459 430 439 10 LDVSAAFYHI 336 B*5201 98 1.79 175 11 422 459 431 439 9 DVSAAFYHI 337 A*6802 46 1.79 81 11 422 459 432 439 8 VSAAFYHI 338 A*3201 18 1.79 32 11 422 459 432 439 8 VSAAFYHI 338 B*1302 28 1.79 50 11 422 459 432 439 8 VSAAFYHI 338 B*5101 8 1.79 15 11 422 459 432 439 8 VSAAFYHI 338 B*5201 96 1.79 172 11 422 459 432 439 8 VSAAFYHI 338 B*5701 65 1.79 116 11 422 459 432 439 8 VSAAFYHI 338 B*5801 64 1.79 115 11 422 459 432 439 8 VSAAFYHI 338 B*5802 49 1.79 88 11 422 459 431 441 11 DVSAAFYHIPL 339 A*2501 33 1.00 33 11 422 459 431 441 11 DVSAAFYHIPL 339 A*2601 51 1.00 51 11 422 459 432 441 10 VSAAFYHIPL 340 A*6802 35 1.00 35 11 422 459 432 441 10 VSAAFYHIPL 340 B*5802 14 1.00 15 11 422 459 433 441 9 SAAFYHIPL 341 B*1402 79 1.00 79 11 422 459 433 441 9 SAAFYHIPL 341 B*3503 34 1.00 34 11 422 459 434 441 8 AAFYHIPL 342 B*0801 64 1.00 65 11 422 459 434 441 8 AAFYHIPL 342 B*1402 57 1.00 57 11 422 459 434 441 8 AAFYHIPL 342 B*3801 6 1.00 6 11 422 459 434 441 8 AAFYHIPL 342 B*3901 32 1.00 33 11 422 459 434 441 8 AAFYHIPL 342 B*4801 63 1.00 64 11 422 459 433 442 10 SAAFYHIPLH 343 A*3001 83 0.25 20 11 422 459 434 444 11 AAFYHIPLHPA 344 A*3001 11 0.89 10 11 422 459 434 444 11 AAFYHIPLHPA 344 B*5501 20 0.89 18 11 422 459 434 444 11 AAFYHIPLHPA 344 B*5601 21 0.89 18 11 422 459 437 444 8 YHIPLHPA 345 B*1402 19 0.89 17 11 422 459 437 444 8 YHIPLHPA 345 B*3901 87 0.89 78 11 422 459 437 445 9 YHIPLHPAA 346 B*1402 18 0.62 11 11 422 459 436 446 11 FYHIPLHPAAM 347 A*2402 19 1.63 31 11 422 459 437 446 10 YHIPLHPAAM 348 B*1402 99 1.63 161 11 422 459 437 446 10 YHIPLHPAAM 348 B*3503 74 1.63 121 11 422 459 437 446 10 YHIPLHPAAM 348 B*3801 86 1.63 140 11 422 459 437 446 10 YHIPLHPAAM 348 B*3901 100 1.63 163 11 422 459 438 446 9 HIPLHPAAM 349 A*2501 73 1.63 120 11 422 459 438 446 9 HIPLHPAAM 349 B*1402 3 1.63 5 11 422 459 439 446 8 IPLHPAAM 350 B*1402 86 1.63 140 11 422 459 439 446 8 IPLHPAAM 350 B*3503 93 1.63 152 11 422 459 439 446 8 IPLHPAAM 350 B*5101 55 1.63 90 11 422 459 439 446 8 IPLHPAAM 350 B*5301 64 1.63 104 11 422 459 439 446 8 IPLHPAAM 350 B*5501 85 1.63 138 11 422 459 439 446 8 IPLHPAAM 350 B*5601 73 1.63 119 11 422 459 439 449 11 IPLHPAAMPHL 351 B*0702 58 1.61 93 11 422 459 439 449 11 IPLHPAAMPHL 351 B*1402 31 1.61 50 11 422 459 439 449 11 IPLHPAAMPHL 351 B*3503 32 1.61 52 11 422 459 439 449 11 IPLHPAAMPHL 351 B*5101 53 1.61 86 11 422 459 439 449 11 IPLHPAAMPHL 351 B*5501 38 1.61 62 11 422 459 441 449 9 LHPAAMPHL 352 B*3801 76 1.61 121 11 422 459 442 449 8 HPAAMPHL 353 B*1402 85 1.61 136 11 422 459 442 449 8 HPAAMPHL 353 B*3503 73 1.61 117 11 422 459 442 449 8 HPAAMPHL 353 B*3901 53 1.61 85 11 422 459 442 449 8 HPAAMPHL 353 B*5101 48 1.61 78 11 422 459 442 449 8 HPAAMPHL 353 B*5301 38 1.61 61 11 422 459 442 449 8 HPAAMPHL 353 B*5501 55 1.61 88 11 422 459 442 449 8 HPAAMPHL 353 B*5601 29 1.61 47 11 422 459 441 450 10 LHPAAMPHLL 354 B*3801 67 1.81 122 11 422 459 442 450 9 HPAAMPHLL 355 B*0702 70 1.81 126 11 422 459 442 450 9 HPAAMPHLL 355 B*1402 93 1.81 168 11 422 459 442 450 9 HPAAMPHLL 355 B*3501 29 1.81 53 11 422 459 442 450 9 HPAAMPHLL 355 B*3503 85 1.81 154 11 422 459 442 450 9 HPAAMPHLL 355 B*3901 97 1.81 176 11 422 459 442 450 9 HPAAMPHLL 355 B*5301 33 1.81 59 11 422 459 442 450 9 HPAAMPHLL 355 B*5501 72 1.81 130 11 422 459 442 450 9 HPAAMPHLL 355 B*5601 58 1.81 104 11 422 459 441 451 11 LHPAAMPHLLI 356 B*3801 61 0.84 51 11 422 459 442 451 10 HPAAMPHLLI 357 B*1402 71 0.84 59 11 422 459 442 451 10 HPAAMPHLLI 357 B*3503 72 0.84 60 11 422 459 442 451 10 HPAAMPHLLI 357 B*3901 38 0.84 31 11 422 459 442 451 10 HPAAMPHLLI 357 B*5201 61 0.84 51 11 422 459 442 451 10 HPAAMPHLLI 357 B*5301 36 0.84 30 11 422 459 442 451 10 HPAAMPHLLI 357 B*5501 84 0.84 70 11 422 459 442 451 10 HPAAMPHLLI 357 B*5601 90 0.84 75 11 422 459 444 451 8 AAMPHLLI 358 A*3201 59 0.84 49 11 422 459 444 451 8 AAMPHLLI 358 B*1302 35 0.84 29 11 422 459 444 451 8 AAMPHLLI 358 B*5101 47 0.84 39 11 422 459 444 451 8 AAMPHLLI 358 B*5201 94 0.84 79 11 422 459 444 451 8 AAMPHLLI 358 B*5801 37 0.84 31 11 422 459 442 452 11 HPAAMPHLLIG 359 A*0201 51 0.32 16 11 422 459 442 452 11 HPAAMPHLLIG 359 A*0206 38 0.32 12 11 422 459 446 453 8 MPHLLIGS 360 A*6802 16 0.77 12 11 422 459 446 453 8 MPHLLIGS 360 B*5601 28 0.77 22 11 422 459 446 454 9 MPHLLIGSS 361 B*5501 37 0.26 10 11 422 459 446 454 9 MPHLLIGSS 361 B*5601 41 0.26 11 11 422 459 446 455 10 MPHLLIGSSG 362 B*0702 35 0.11 4 11 422 459 446 455 10 MPHLLIGSSG 362 B*3501 40 0.11 4 11 422 459 446 455 10 MPHLLIGSSG 362 B*5501 3 0.11 0 11 422 459 446 455 10 MPHLLIGSSG 362 B*5601 18 0.11 2 11 422 459 446 456 11 MPHLLIGSSGL 363 B*0702 93 1.81 168 11 422 459 446 456 11 MPHLLIGSSGL 363 B*0801 44 1.81 80 11 422 459 446 456 11 MPHLLIGSSGL 363 B*1402 92 1.81 167 11 422 459 446 456 11 MPHLLIGSSGL 363 B*3501 27 1.81 48 11 422 459 446 456 11 MPHLLIGSSGL 363 B*3503 70 1.81 127 11 422 459 446 456 11 MPHLLIGSSGL 363 B*3901 62 1.81 113 11 422 459 446 456 11 MPHLLIGSSGL 363 B*5101 40 1.81 73 11 422 459 446 456 11 MPHLLIGSSGL 363 B*5301 18 1.81 33 11 422 459 446 456 11 MPHLLIGSSGL 363 B*5501 71 1.81 129 11 422 459 446 456 11 MPHLLIGSSGL 363 B*5601 53 1.81 95 11 422 459 448 456 9 HLLIGSSGL 364 B*1502 83 1.81 151 11 422 459 449 456 8 LLIGSSGL 365 B*0702 77 1.81 139 11 422 459 448 458 11 HLLIGSSGLSR 366 A*0301 11 1.14 13 11 422 459 448 458 11 HLLIGSSGLSR 366 A*3101 19 1.14 22 11 422 459 448 458 11 HLLIGSSGLSR 366 A*3303 17 1.14 19 11 422 459 448 458 11 HLLIGSSGLSR 366 A*7401 62 1.14 71 11 422 459 449 458 10 LLIGSSGLSR 367 A*7401 6 1.14 7 11 422 459 449 459 11 LLIGSSGLSRY 368 A*2501 57 1.50 85 11 422 459 449 459 11 LLIGSSGLSRY 368 A*2601 77 1.50 115 11 422 459 449 459 11 LLIGSSGLSRY 368 A*2902 89 1.50 133 11 422 459 449 459 11 LLIGSSGLSRY 368 A*3002 66 1.50 99 11 422 459 449 459 11 LLIGSSGLSRY 368 B*1501 81 1.50 122 11 422 459 449 459 11 LLIGSSGLSRY 368 B*1502 57 1.50 86 11 422 459 449 459 11 LLIGSSGLSRY 368 B*1525 41 1.50 61 11 422 459 449 459 11 LLIGSSGLSRY 368 B*4601 28 1.50 42 11 422 459 450 459 10 LIGSSGLSRY 369 A*0101 45 1.50 68 11 422 459 450 459 10 LIGSSGLSRY 369 A*3002 35 1.50 53 11 422 459 451 459 9 IGSSGLSRY 370 A*3002 94 1.50 141 11 422 459 452 459 8 GSSGLSRY 371 A*0101 83 1.50 124 11 422 459 452 459 8 GSSGLSRY 371 A*3002 77 1.50 116 11 422 459 Cumulative Class I-BCI score: 12384 427 435 9 WLSLDVSAA 328 A*0201 14 0.74 10 12 427 459 426 436 11 SWLSLDVSAAF 329 A*2301 91 1.90 174 12 427 459 426 436 11 SWLSLDVSAAF 329 A*2402 93 1.90 177 12 427 459 426 436 11 SWLSLDVSAAF 329 A*2902 32 1.90 60 12 427 459 426 436 11 SWLSLDVSAAF 329 B*1801 38 1.90 72 12 427 459 427 436 10 WLSLDVSAAF 330 B*1501 72 1.90 137 12 427 459 427 436 10 WLSLDVSAAF 330 B*1502 89 1.90 169 12 427 459 427 436 10 WLSLDVSAAF 330 B*1525 54 1.90 103 12 427 459 428 436 9 LSLDVSAAF 331 B*1501 73 1.90 140 12 427 459 428 436 9 LSLDVSAAF 331 B*1525 76 1.90 145 12 427 459 428 436 9 LSLDVSAAF 331 B*3501 69 1.90 132 12 427 459 428 436 9 LSLDVSAAF 331 B*3503 51 1.90 98 12 427 459 428 436 9 LSLDVSAAF 331 B*4601 75 1.90 144 12 427 459 428 436 9 LSLDVSAAF 331 B*5801 63 1.90 119 12 427 459 427 437 11 WLSLDVSAAFY 332 A*0101 74 1.81 133 12 427 459 427 437 11 WLSLDVSAAFY 332 A*2601 38 1.81 69 12 427 459 427 437 11 WLSLDVSAAFY 332 A*2902 75 1.81 135 12 427 459 427 437 11 WLSLDVSAAFY 332 B*1502 22 1.81 40 12 427 459 428 437 10 LSLDVSAAFY 333 A*0101 100 1.81 181 12 427 459 428 437 10 LSLDVSAAFY 333 A*2902 83 1.81 149 12 427 459 428 437 10 LSLDVSAAFY 333 A*3002 99 1.81 178 12 427 459 428 437 10 LSLDVSAAFY 333 B*1501 22 1.81 40 12 427 459 428 437 10 LSLDVSAAFY 333 B*4601 69 1.81 124 12 427 459 428 437 10 LSLDVSAAFY 333 B*5802 57 1.81 102 12 427 459 429 437 9 SLDVSAAFY 334 A*0101 85 1.81 153 12 427 459 429 437 9 SLDVSAAFY 334 A*3002 59 1.81 107 12 427 459 430 437 8 LDVSAAFY 335 B*3501 31 1.81 55 12 427 459 430 439 10 LDVSAAFYHI 336 B*1301 96 1.79 171 12 427 459 430 439 10 LDVSAAFYHI 336 B*1302 49 1.79 88 12 427 459 430 439 10 LDVSAAFYHI 336 B*3701 57 1.79 102 12 427 459 430 439 10 LDVSAAFYHI 336 B*4901 57 1.79 101 12 427 459 430 439 10 LDVSAAFYHI 336 B*5201 98 1.79 175 12 427 459 431 439 9 DVSAAFYHI 337 A*6802 46 1.79 81 12 427 459 432 439 8 VSAAFYHI 338 A*3201 18 1.79 32 12 427 459 432 439 8 VSAAFYHI 338 B*1302 28 1.79 50 12 427 459 432 439 8 VSAAFYHI 338 B*5101 8 1.79 15 12 427 459 432 439 8 VSAAFYHI 338 B*5201 96 1.79 172 12 427 459 432 439 8 VSAAFYHI 338 B*5701 65 1.79 116 12 427 459 432 439 8 VSAAFYHI 338 B*5801 64 1.79 115 12 427 459 432 439 8 VSAAFYHI 338 B*5802 49 1.79 88 12 427 459 431 441 11 DVSAAFYHIPL 339 A*2501 33 1.00 33 12 427 459 431 441 11 DVSAAFYHIPL 339 A*2601 51 1.00 51 12 427 459 432 441 10 VSAAFYHIPL 340 A*6802 35 1.00 35 12 427 459 432 441 10 VSAAFYHIPL 340 B*5802 14 1.00 15 12 427 459 433 441 9 SAAFYHIPL 341 B*1402 79 1.00 79 12 427 459 433 441 9 SAAFYHIPL 341 B*3503 34 1.00 34 12 427 459 434 441 8 AAFYHIPL 342 B*0801 64 1.00 65 12 427 459 434 441 8 AAFYHIPL 342 B*1402 57 1.00 57 12 427 459 434 441 8 AAFYHIPL 342 B*3801 6 1.00 6 12 427 459 434 441 8 AAFYHIPL 342 B*3901 32 1.00 33 12 427 459 434 441 8 AAFYHIPL 342 B*4801 63 1.00 64 12 427 459 433 442 10 SAAFYHIPLH 343 A*3001 83 0.25 20 12 427 459 434 444 11 AAFYHIPLHPA 344 A*3001 11 0.89 10 12 427 459 434 444 11 AAFYHIPLHPA 344 B*5501 20 0.89 18 12 427 459 434 444 11 AAFYHIPLHPA 344 B*5601 21 0.89 18 12 427 459 437 444 8 YHIPLHPA 345 B*1402 19 0.89 17 12 427 459 437 444 8 YHIPLHPA 345 B*3901 87 0.89 78 12 427 459 437 445 9 YHIPLHPAA 346 B*1402 18 0.62 11 12 427 459 436 446 11 FYHIPLHPAAM 347 A*2402 19 1.63 31 12 427 459 437 446 10 YHIPLHPAAM 348 B*1402 99 1.63 161 12 427 459 437 446 10 YHIPLHPAAM 348 B*3503 74 1.63 121 12 427 459 437 446 10 YHIPLHPAAM 348 B*3801 86 1.63 140 12 427 459 437 446 10 YHIPLHPAAM 348 B*3901 100 1.63 163 12 427 459 438 446 9 HIPLHPAAM 349 A*2501 73 1.63 120 12 427 459 438 446 9 HIPLHPAAM 349 B*1402 3 1.63 5 12 427 459 439 446 8 IPLHPAAM 350 B*1402 86 1.63 140 12 427 459 439 446 8 IPLHPAAM 350 B*3503 93 1.63 152 12 427 459 439 446 8 IPLHPAAM 350 B*5101 55 1.63 90 12 427 459 439 446 8 IPLHPAAM 350 B*5301 64 1.63 104 12 427 459 439 446 8 IPLHPAAM 350 B*5501 85 1.63 138 12 427 459 439 446 8 IPLHPAAM 350 B*5601 73 1.63 119 12 427 459 439 449 11 IPLHPAAMPHL 351 B*0702 58 1.61 93 12 427 459 439 449 11 IPLHPAAMPHL 351 B*1402 31 1.61 50 12 427 459 439 449 11 IPLHPAAMPHL 351 B*3503 32 1.61 52 12 427 459 439 449 11 IPLHPAAMPHL 351 B*5101 53 1.61 86 12 427 459 439 449 11 IPLHPAAMPHL 351 B*5501 38 1.61 62 12 427 459 441 449 9 LHPAAMPHL 352 B*3801 76 1.61 121 12 427 459 442 449 8 HPAAMPHL 353 B*1402 85 1.61 136 12 427 459 442 449 8 HPAAMPHL 353 B*3503 73 1.61 117 12 427 459 442 449 8 HPAAMPHL 353 B*3901 53 1.61 85 12 427 459 442 449 8 HPAAMPHL 353 B*5101 48 1.61 78 12 427 459 442 449 8 HPAAMPHL 353 B*5301 38 1.61 61 12 427 459 442 449 8 HPAAMPHL 353 B*5501 55 1.61 88 12 427 459 442 449 8 HPAAMPHL 353 B*5601 29 1.61 47 12 427 459 441 450 10 LHPAAMPHLL 354 B*3801 67 1.81 122 12 427 459 442 450 9 HPAAMPHLL 355 B*0702 70 1.81 126 12 427 459 442 450 9 HPAAMPHLL 355 B*1402 93 1.81 168 12 427 459 442 450 9 HPAAMPHLL 355 B*3501 29 1.81 53 12 427 459 442 450 9 HPAAMPHLL 355 B*3503 85 1.81 154 12 427 459 442 450 9 HPAAMPHLL 355 B*3901 97 1.81 176 12 427 459 442 450 9 HPAAMPHLL 355 B*5301 33 1.81 59 12 427 459 442 450 9 HPAAMPHLL 355 B*5501 72 1.81 130 12 427 459 442 450 9 HPAAMPHLL 355 B*5601 58 1.81 104 12 427 459 441 451 11 LHPAAMPHLLI 356 B*3801 61 0.84 51 12 427 459 442 451 10 HPAAMPHLLI 357 B*1402 71 0.84 59 12 427 459 442 451 10 HPAAMPHLLI 357 B*3503 72 0.84 60 12 427 459 442 451 10 HPAAMPHLLI 357 B*3901 38 0.84 31 12 427 459 442 451 10 HPAAMPHLLI 357 B*5201 61 0.84 51 12 427 459 442 451 10 HPAAMPHLLI 357 B*5301 36 0.84 30 12 427 459 442 451 10 HPAAMPHLLI 357 B*5501 84 0.84 70 12 427 459 442 451 10 HPAAMPHLLI 357 B*5601 90 0.84 75 12 427 459 444 451 8 AAMPHLLI 358 A*3201 59 0.84 49 12 427 459 444 451 8 AAMPHLLI 358 B*1302 35 0.84 29 12 427 459 444 451 8 AAMPHLLI 358 B*5101 47 0.84 39 12 427 459 444 451 8 AAMPHLLI 358 B*5201 94 0.84 79 12 427 459 444 451 8 AAMPHLLI 358 B*5801 37 0.84 31 12 427 459 442 452 11 HPAAMPHLLIG 359 A*0201 51 0.32 16 12 427 459 442 452 11 HPAAMPHLLIG 359 A*0206 38 0.32 12 12 427 459 446 453 8 MPHLLIGS 360 A*6802 16 0.77 12 12 427 459 446 453 8 MPHLLIGS 360 B*5601 28 0.77 22 12 427 459 446 454 9 MPHLLIGSS 361 B*5501 37 0.26 10 12 427 459 446 454 9 MPHLLIGSS 361 B*5601 41 0.23 11 12 427 459 446 455 10 MPHLLIGSSG 362 B*0702 35 0.11 4 12 427 459 446 455 10 MPHLLIGSSG 362 B*3501 40 0.11 4 12 427 459 446 455 10 MPHLLIGSSG 362 B*5501 3 0.11 0 12 427 459 446 455 10 MPHLLIGSSG 362 B*5601 18 0.11 2 12 427 459 446 456 11 MPHLLIGSSGL 363 B*0702 93 1.81 168 12 427 459 446 456 11 MPHLLIGSSGL 363 B*0801 44 1.81 80 12 427 459 446 456 11 MPHLLIGSSGL 363 B*1402 92 1.81 167 12 427 459 446 456 11 MPHLLIGSSGL 363 B*3501 27 1.81 48 12 427 459 446 456 11 MPHLLIGSSGL 363 B*3503 70 1.81 127 12 427 459 446 456 11 MPHLLIGSSGL 363 B*3901 62 1.81 113 12 427 459 446 456 11 MPHLLIGSSGL 363 B*5101 40 1.81 73 12 427 459 446 456 11 MPHLLIGSSGL 363 B*5301 18 1.81 33 12 427 459 446 456 11 MPHLLIGSSGL 363 B*5501 71 1.81 129 12 427 459 446 456 11 MPHLLIGSSGL 363 B*5601 53 1.81 95 12 427 459 448 456 9 HLLIGSSGL 364 B*1502 83 1.81 151 12 427 459 449 456 8 LLIGSSGL 365 B*0702 77 1.81 139 12 427 459 448 458 11 HLLIGSSGLSR 366 A*0301 11 1.14 13 12 427 459 448 458 11 HLLIGSSGLSR 366 A*3101 19 1.14 22 12 427 459 448 458 11 HLLIGSSGLSR 366 A*3303 17 1.14 19 12 427 459 448 458 11 HLLIGSSGLSR 366 A*7401 62 1.14 71 12 427 459 449 458 10 LLIGSSGLSR 367 A*7401 6 1.14 7 12 427 459 449 459 11 LLIGSSGLSRY 368 A*2501 57 1.50 85 12 427 459 449 459 11 LLIGSSGLSRY 368 A*2601 77 1.50 115 12 427 459 449 459 11 LLIGSSGLSRY 368 A*2902 89 1.50 133 12 427 459 449 459 11 LLIGSSGLSRY 368 A*3002 66 1.50 99 12 427 459 449 459 11 LLIGSSGLSRY 368 B*1501 81 1.50 122 12 427 459 449 459 11 LLIGSSGLSRY 368 B*1502 57 1.50 86 12 427 459 449 459 11 LLIGSSGLSRY 368 B*1525 41 1.50 61 12 427 459 449 459 11 LLIGSSGLSRY 368 B*4601 28 1.50 42 12 427 459 450 459 10 LIGSSGLSRY 369 A*0101 45 1.50 68 12 427 459 450 459 10 LIGSSGLSRY 369 A*3002 35 1.50 53 12 427 459 451 459 9 IGSSGLSRY 370 A*3002 94 1.50 141 12 427 459 452 459 8 GSSGLSRY 371 A*0101 83 1.50 124 12 427 459 452 459 8 GSSGLSRY 371 A*3002 77 1.50 116 12 427 459 Cumulative Class I-BCI score: 12198 485 492 8 SRQLYVSL 372 B*1402 84 1.59 134 13 481 514 485 492 8 SRQLYVSL 372 B*2702 89 1.59 142 13 481 514 485 492 8 SRQLYVSL 372 B*3901 86 1.59 137 13 481 514 485 492 8 SRQLYVSL 372 B*4801 2 1.59 3 13 481 514 484 493 10 CSRQLYVSLM 373 B*4601 43 1.55 66 13 481 514 485 493 9 SRQLYVSLM 374 B*2702 88 1.55 137 13 481 514 485 493 9 SRQLYVSLM 374 B*2705 85 1.55 132 13 481 514 486 493 8 RQLYVSLM 375 A*3201 53 1.55 82 13 481 514 486 493 8 RQLYVSLM 375 B*1301 85 1.55 131 13 481 514 486 493 8 RQLYVSLM 375 B*1302 13 1.55 20 13 481 514 486 493 8 RQLYVSLM 375 B*1402 15 1.55 24 13 481 514 486 493 8 RQLYVSLM 375 B*1501 48 1.55 75 13 481 514 486 493 8 RQLYVSLM 375 B*1525 75 1.55 116 13 481 514 486 493 8 RQLYVSLM 375 B*2702 73 1.55 114 13 481 514 486 493 8 RQLYVSLM 375 B*3901 51 1.55 79 13 481 514 486 493 8 RQLYVSLM 375 B*4801 94 1.55 146 13 481 514 485 494 10 SRQLYVSLML 376 B*1402 49 1.55 77 13 481 514 485 494 10 SRQLYVSLML 376 B*2702 87 1.55 135 13 481 514 485 494 10 SRQLYVSLML 376 B*2705 88 1.55 137 13 481 514 485 494 10 SRQLYVSLML 376 B*3901 52 1.55 81 13 481 514 486 494 9 RQLYVSLML 377 A*0206 19 1.55 29 13 481 514 486 494 9 RQLYVSLML 377 A*3201 79 1.55 122 13 481 514 486 494 9 RQLYVSLML 377 B*1301 80 1.55 125 13 481 514 486 494 9 RQLYVSLML 377 B*1302 21 1.55 33 13 481 514 486 494 9 RQLYVSLML 377 B*2702 72 1.55 112 13 481 514 486 494 9 RQLYVSLML 377 B*2705 52 1.55 81 13 481 514 486 494 9 RQLYVSLML 377 B*4001 52 1.55 81 13 481 514 486 494 9 RQLYVSLML 377 B*4801 96 1.55 149 13 481 514 487 494 8 QLYVSLML 378 A*0201 58 1.55 90 13 481 514 485 495 11 SRQLYVSLMLL 379 B*1402 16 1.34 22 13 481 514 485 495 11 SRQLYVSLMLL 379 B*2702 98 1.34 131 13 481 514 485 495 11 SRQLYVSLMLL 379 B*2705 25 1.34 34 13 481 514 486 495 10 RQLYVSLMLL 380 A*0206 48 1.34 64 13 481 514 486 495 10 RQLYVSLMLL 380 B*1301 87 1.34 117 13 481 514 486 495 10 RQLYVSLMLL 380 B*1302 34 1.34 45 13 481 514 486 495 10 RQLYVSLMLL 380 B*2702 86 1.34 115 13 481 514 486 495 10 RQLYVSLMLL 380 B*3801 10 1.34 14 13 481 514 486 495 10 RQLYVSLMLL 380 B*3901 43 1.34 57 13 481 514 486 495 10 RQLYVSLMLL 380 B*4801 100 1.34 134 13 481 514 488 495 8 LYVSLMLL 381 A*2301 72 1.34 97 13 481 514 488 495 8 LYVSLMLL 381 A*2402 72 1.34 96 13 481 514 488 495 8 LYVSLMLL 381 B*0702 91 1.34 122 13 481 514 486 496 11 RQLYVSLMLLY 382 A*0301 61 1.80 109 13 481 514 486 496 11 RQLYVSLMLLY 382 B*1501 47 1.80 84 13 481 514 486 496 11 RQLYVSLMLLY 382 B*1525 68 1.80 122 13 481 514 486 496 11 RQLYVSLMLLY 382 B*2702 84 1.80 152 13 481 514 486 496 11 RQLYVSLMLLY 382 B*2705 76 1.80 137 13 481 514 487 496 10 QLYVSLMLLY 383 B*4403 44 1.80 79 13 481 514 488 496 9 LYVSLMLLY 384 A*2902 98 1.80 177 13 481 514 489 496 8 YVSLMLLY 385 A*0101 94 1.80 170 13 481 514 489 496 8 YVSLMLLY 385 A*2501 90 1.80 162 13 481 514 489 496 8 YVSLMLLY 385 A*2601 97 1.80 176 13 481 514 489 496 8 YVSLMLLY 385 A*3002 87 1.80 157 13 481 514 489 496 8 YVSLMLLY 385 B*3501 88 1.80 159 13 481 514 489 496 8 YVSLMLLY 385 B*4601 56 1.80 100 13 481 514 487 497 11 QLYVSLMLLYK 386 A*1101 85 1.07 91 13 481 514 487 497 11 QLYVSLMLLYK 386 A*7401 61 1.07 65 13 481 514 488 497 10 LYVSLMLLYK 387 A*0301 25 1.07 26 13 481 514 489 497 9 YVSLMLLYK 388 A*0301 67 1.07 72 13 481 514 489 497 9 YVSLMLLYK 388 A*1101 91 1.07 98 13 481 514 489 497 9 YVSLMLLYK 388 A*6801 66 1.07 71 13 481 514 489 497 9 YVSLMLLYK 388 A*7401 12 1.07 13 13 481 514 490 497 8 VSLMLLYK 389 A*0301 80 1.07 86 13 481 514 490 497 8 VSLMLLYK 389 A*1101 98 1.07 105 13 481 514 490 497 8 VSLMLLYK 389 A*7401 35 1.07 38 13 481 514 489 499 11 YVSLMLLYKTY 390 A*0101 81 1.86 151 13 481 514 489 499 11 YVSLMLLYKTY 390 A*2501 55 1.86 102 13 481 514 489 499 11 YVSLMLLYKTY 390 A*2601 74 1.86 138 13 481 514 489 499 11 YVSLMLLYKTY 390 A*2902 86 1.86 159 13 481 514 489 499 11 YVSLMLLYKTY 390 A*3002 42 1.86 78 13 481 514 489 499 11 YVSLMLLYKTY 390 B*1502 31 1.86 58 13 481 514 489 499 11 YVSLMLLYKTY 390 B*4601 13 1.86 24 13 481 514 490 499 10 VSLMLLYKTY 391 A*0101 75 1.86 140 13 481 514 490 499 10 VSLMLLYKTY 391 A*3002 48 1.86 89 13 481 514 490 499 10 VSLMLLYKTY 391 B*5802 38 1.86 70 13 481 514 492 499 8 LMLLYKTY 392 A*2902 52 1.86 97 13 481 514 492 499 8 LMLLYKTY 392 B*1525 19 1.86 35 13 481 514 492 499 8 LMLLYKTY 392 B*3501 57 1.86 106 13 481 514 491 500 10 SLMLLYKTYG 393 A*0201 9 0.13 1 13 481 514 491 501 11 SLMLLYKTYGW 394 A*3201 68 1.93 132 13 481 514 492 501 10 LMLLYKTYGW 395 A*2301 17 1.93 33 13 481 514 492 501 10 LMLLYKTYGW 395 B*5301 28 1.93 54 13 481 514 492 501 10 LMLLYKTYGW 395 B*5802 36 1.93 70 13 481 514 493 501 9 MLLYKTYGW 396 A*3201 92 1.93 179 13 481 514 493 501 9 MLLYKTYGW 396 B*5701 36 1.93 70 13 481 514 493 501 9 MLLYKTYGW 396 B*5801 31 1.93 59 13 481 514 494 501 8 LLYKTYGW 397 A*3201 50 1.93 97 13 481 514 494 501 8 LLYKTYGW 397 B*5701 47 1.93 91 13 481 514 494 501 8 LLYKTYGW 397 B*5801 53 1.93 102 13 481 514 494 501 8 LLYKTYGW 397 B*5802 6 1.93 11 13 481 514 492 502 11 LMLLYKTYGWK 398 A*0206 15 0.71 10 13 481 514 492 502 11 LMLLYKTYGWK 398 A*0301 79 0.71 56 13 481 514 492 502 11 LMLLYKTYGWK 398 A*1101 20 0.71 14 13 481 514 492 502 11 LMLLYKTYGWK 398 A*7401 34 0.71 24 13 481 514 493 502 10 MLLYKTYGWK 399 A*0301 97 0.71 69 13 481 514 493 502 10 MLLYKTYGWK 399 A*1101 26 0.71 19 13 481 514 493 502 10 MLLYKTYGWK 399 A*7401 48 0.71 34 13 481 514 494 502 9 LLYKTYGWK 400 A*0301 95 0.71 68 13 481 514 495 502 8 LYKTYGWK 401 A*3001 24 0.71 17 13 481 514 493 503 11 MLLYKTYGWKL 402 A*3201 52 0.71 100 13 481 514 493 503 11 MLLYKTYGWKL 402 B*0801 98 0.71 192 13 481 514 493 503 11 MLLYKTYGWKL 402 B*1402 9 0.71 18 13 481 514 494 503 10 LLYKtYGWKL 403 A*0201 82 0.71 58 13 481 514 495 503 9 LYKTYGWKL 404 A*2301 24 1.95 47 13 481 514 495 503 9 LYKTYGWKL 404 A*2402 60 1.95 116 13 481 514 496 503 8 YKTYGWKL 405 B*3901 84 1.95 165 13 481 514 495 504 10 LYKTYGWKLH 406 A*3201 35 0.88 31 13 481 514 497 504 8 KTYGWKLH 407 A*0301 59 0.88 52 13 481 514 497 504 8 KTYGWKLH 407 A*7401 5 0.88 4 13 481 514 495 505 11 LYKTYGWKLHL 408 A*2301 45 1.71 77 13 481 514 495 505 11 LYKTYGWKLHL 408 A*2402 51 1.71 87 13 481 514 496 505 10 YKTYGWKLHL 409 B*3901 12 1.71 20 13 481 514 497 505 9 KTYGWKLHL 410 A*3201 86 1.71 148 13 481 514 497 505 9 KTYGWKLHL 410 A*7401 4 1.71 6 13 481 514 497 505 9 KTYGWKLHL 410 B*5701 68 1.71 117 13 481 514 497 505 9 KTYGWKLHL 410 B*5801 47 1.71 81 13 481 514 497 505 9 KTYGWKLHL 410 B*5802 28 1.71 47 13 481 514 498 505 8 TYGWKLHL 411 A*2301 64 1.71 109 13 481 514 498 505 8 TYGWKLHL 411 A*2402 63 1.71 108 13 481 514 496 506 11 YKTYGWKLHLY 412 A*2902 30 1.90 57 13 481 514 497 506 10 KTYGWKLHLY 413 A*0101 77 1.90 147 13 481 514 497 506 10 KTYGWKLHLY 413 A*0301 92 1.90 175 13 481 514 497 506 10 KTYGWKLHLY 413 A*2501 78 1.90 148 13 481 514 497 506 10 KTYGWKLHLY 413 A*3002 97 1.90 185 13 481 514 497 506 10 KTYGWKLHLY 413 A*7401 85 1.90 162 13 481 514 497 506 10 KTYGWKLHLY 413 B*5802 83 1.90 157 13 481 514 498 506 9 TYGWKLHLY 414 A*2402 37 1.90 70 13 481 514 498 506 9 TYGWKLHLY 414 A*2902 90 1.90 172 13 481 514 498 506 9 TYGWKLHLY 414 A*3002 70 1.90 134 13 481 514 499 506 8 YGWKLHLY 415 A*2902 97 1.90 184 13 481 514 499 506 8 YGWKLHLY 415 A*3002 76 1.90 145 13 481 514 499 506 8 YGWKLHLY 415 B*3501 55 1.90 104 13 481 514 500 510 11 GWKLHLYSHPI 416 B*0801 32 0.99 32 13 481 514 501 510 10 WKLHLYSHPI 417 B*1301 54 0.99 53 13 481 514 501 510 10 WKLHLYSHPI 417 B*1302 27 0.99 27 13 481 514 501 510 10 WKLHLYSHPI 417 B*3701 43 0.99 42 13 481 514 501 510 10 WKLHLYSHPI 417 B*3901 69 0.99 68 13 481 514 501 510 10 WKLHLYSHPI 417 B*5201 78 0.99 78 13 481 514 502 510 9 KLHLYSHPI 418 A*0201 49 0.99 48 13 481 514 502 510 9 KLHLYSHPI 418 A*3201 77 0.99 77 13 481 514 503 510 8 LHLYSHPI 419 B*1402 78 0.99 77 13 481 514 503 510 8 LHLYSHPI 419 B*2702 10 0.99 10 13 481 514 503 510 8 LHLYSHPI 419 B*3801 92 0.99 91 13 481 514 503 510 8 LHLYSHPI 419 B*5101 52 0.99 51 13 481 514 503 510 8 LHLYSHPI 419 B*5201 84 0.99 84 13 481 514 502 511 10 KLHLYSHPIV 420 A*0201 13 0.55 7 13 481 514 502 511 10 KLHLYSHPIV 420 A*3001 98 0.55 54 13 481 514 503 511 9 LHLYSHPIV 421 B*5101 3 0.55 2 13 481 514 504 511 8 HLYSHPIV 422 A*0201 56 0.55 30 13 481 514 504 511 8 HLYSHPIV 422 B*0801 25 0.55 14 13 481 514 502 512 11 KLHLYSHPIVL 423 A*3201 41 1.95 80 13 481 514 502 512 11 KLHLYSHPIVL 423 B*0801 27 1.95 53 13 481 514 502 512 11 KLHLYSHPIVL 423 B*4801 56 1.95 109 13 481 514 503 512 10 LHLYSHPIVL 424 B*1402 91 1.95 177 13 481 514 503 512 10 LHLYSHPIVL 424 B*3801 78 1.95 151 13 481 514 503 512 10 LHLYSHPIVL 424 B*3901 83 1.95 162 13 481 514 504 512 9 HLYSHPIVL 425 A*0201 18 1.95 35 13 481 514 504 512 9 HLYSHPIVL 425 B*1402 83 1.95 162 13 481 514 504 512 9 HLYSHPIVL 425 B*1502 24 1.95 47 13 481 514 504 512 9 HLYSHPIVL 425 B*3901 91 1.95 177 13 481 514 505 512 8 LYSHPIVL 426 A*2301 22 1.95 44 13 481 514 505 512 8 LYSHPIVL 426 A*2402 46 1.95 89 13 481 514 504 514 11 HLYSHPIVLGF 427 A*2501 43 1.62 69 13 481 514 504 514 11 HLYSHPIVLGF 427 A*2601 10 1.62 17 13 481 514 504 514 11 HLYSHPIVLGF 427 A*3201 100 1.62 162 13 481 514 504 514 11 HLYSHPIVLGF 427 B*1402 30 1.62 49 13 481 514 504 514 11 HLYSHPIVLGF 427 B*1501 80 1.62 129 13 481 514 504 514 11 HLYSHPIVLGF 427 B*1502 96 1.62 156 13 481 514 504 514 11 HLYSHPIVLGF 427 B*1525 90 1.62 145 13 481 514 505 514 10 LYSHPIVLGF 428 A*2301 84 1.62 136 13 481 514 505 514 10 LYSHPIVLGF 428 A*2402 86 1.62 139 13 481 514 505 514 10 LYSHPIVLGF 428 A*2902 76 1.62 123 13 481 514 506 514 9 YSHPIVLGF 429 B*4601 64 1.62 103 13 481 514 506 514 9 YSHPIVLGF 429 B*5801 71 1.62 115 13 481 514 506 514 9 YSHPIVLGF 429 B*5802 59 1.62 96 13 481 514 Cumulative BCI Class Iscore: 15733 524 531 8 SPFLLAQF 432 B*1402 67 1.59 106 14 524 559 524 531 8 SPFLLAQF 432 B*1502 6 1.59 9 14 524 559 524 531 8 SPFLLAQF 432 B*3503 61 1.59 97 14 524 559 524 531 8 SPFLLAQF 432 B*5301 72 1.59 115 14 524 559 524 532 9 SPFLLAQFT 433 B*5601 17 0.30 5 14 524 559 524 533 10 SPFLLAQFTS 434 A*3201 5 0.76 3 14 524 559 524 533 10 SPFLLAQFTS 434 B*3501 1 0.76 1 14 524 559 524 533 10 SPFLLAQFTS 434 B*5601 27 0.76 21 14 524 559 526 533 8 FLLAQFTS 435 A*0201 42 0.76 32 14 524 559 524 534 11 SPFLLAQFTSA 436 B*0702 46 0.92 43 14 524 559 524 534 11 SPFLLAQFTSA 436 B*3503 3 0.92 2 14 524 559 524 534 11 SPFLLAQFTSA 436 B*5101 25 0.92 23 14 524 559 524 534 11 SPFLLAQFTSA 436 B*5501 98 0.92 90 14 524 559 524 534 11 SPFLLAQFTSA 436 B*5601 95 0.92 88 14 524 559 526 534 9 FLLAQFTSA 437 A*0201 84 0.92 78 14 524 559 526 534 9 FLLAQFTSA 437 A*0206 98 0.92 91 14 524 559 526 534 9 FLLAQFTSA 437 B*0801 78 0.92 72 14 524 559 526 535 10 FLLAQFTSAI 438 A*0201 76 0.94 71 14 524 559 526 535 10 FLLAQFTSAI 438 A*0206 79 0.94 75 14 524 559 526 535 10 FLLAQFTSAI 438 B*1302 11 0.94 11 14 524 559 526 535 10 FLLAQFTSAI 438 B*3801 47 0.94 44 14 524 559 526 535 10 FLLAQFTSAI 438 B*4601 11 0.94 11 14 524 559 526 535 10 FLLAQFTSAI 438 B*5201 14 0.94 13 14 524 559 527 535 9 LLAQFTSAI 439 A*3201 3 0.94 3 14 524 559 527 535 9 LLAQFTSAI 439 B*1525 17 0.94 16 14 524 559 527 535 9 LLAQFTSAI 439 B*5501 19 0.94 18 14 524 559 528 535 8 LAQFTSAI 440 B*5101 62 0.94 58 14 524 559 528 535 8 LAQFTSAI 440 B*5201 76 0.94 72 14 524 559 528 535 8 LAQFTSAI 440 B*5301 5 0.94 5 14 524 559 527 537 11 LLAQFTSAICS 441 A*6802 22 0.41 9 14 524 559 528 538 11 LAQFTSAICSV 442 B*5101 13 1.40 19 14 524 559 528 538 11 LAQFTSAICSV 442 B*5201 12 1.40 16 14 524 559 529 538 10 AQFTsAICSV 443 A*0201 55 1.40 77 14 524 559 529 538 10 AQFTSAICSV 443 A*0206 85 1.40 119 14 524 559 529 538 10 AQFTSAICSV 443 B*1301 83 1.40 116 14 524 559 529 538 10 AQFTSAICSV 443 B*1302 46 1.40 65 14 524 559 529 538 10 AQFTSAICSV 443 B*3701 14 1.40 20 14 524 559 529 538 10 AQFTSAICSV 443 B*3901 10 1.40 15 14 524 559 529 538 10 AQFTSAICSV 443 B*4801 77 1.40 108 14 524 559 529 538 10 AQFTSAICSV 443 B*4901 30 1.40 43 14 524 559 529 538 10 AQFTSAICSV 443 B*5001 64 1.40 90 14 524 559 529 538 10 AQFTSAICSV 443 B*5201 82 1.40 115 14 524 559 531 538 8 FTSAICSV 444 A*2501 82 1.40 114 14 524 559 531 538 8 FTSAICSV 444 A*2601 49 1.40 68 14 524 559 529 539 11 AQFTSAICSVV 445 B*1301 75 1.34 100 14 524 559 529 539 11 AQFTSAICSVV 445 B*1302 41 1.34 55 14 524 559 529 539 11 AQFTSAICSVV 445 B*4002 20 1.34 27 14 524 559 529 539 11 AQFTSAICSVV 445 B*4801 62 1.34 83 14 524 559 529 539 11 AQFTSAICSVV 445 B*4901 26 1.34 35 14 524 559 529 539 11 AQFTSAICSVV 445 B*5001 60 1.34 81 14 524 559 529 539 11 AQFTSAICSVV 445 B*5201 53 1.34 71 14 524 559 531 539 9 FTSAICSVV 446 A*6802 49 1.34 65 14 524 559 531 539 9 FTSAICSVV 446 B*4601 31 1.34 42 14 524 559 531 539 9 FTSAICSVV 446 B*5201 2 1.34 3 14 524 559 531 539 9 FTSAICSVV 446 B*5601 4 1.34 5 14 524 559 530 540 11 QFTSAICSVVR 447 A*3303 30 1.19 35 14 524 559 531 540 10 FTSAICSVVR 448 A*3101 38 1.19 45 14 524 559 531 540 10 FTSAICSVVR 448 A*3303 92 1.19 109 14 524 559 531 540 10 FTSAICSVVR 448 A*6801 100 1.19 119 14 524 559 531 540 10 FTSAICSVVR 448 A*7401 68 1.19 81 14 524 559 531 540 10 FTSAICSVVR 448 B*5701 23 1.19 27 14 524 559 532 540 9 TSAICSVVR 449 A*6801 82 1.19 98 14 524 559 533 540 8 SAICSVVR 450 A*3101 11 1.19 14 14 524 559 533 540 8 SAICSVVR 450 A*3303 39 1.19 47 14 524 559 533 540 8 SAICSVVR 450 A*6801 81 1.19 96 14 524 559 531 541 11 FTSAICSVVRR 451 A*1101 2 1.69 4 14 524 559 531 541 11 FTSAICSVVRR 451 A*3101 32 1.69 54 14 524 559 531 541 11 FTSAICSVVRR 451 A*3303 96 1.69 162 14 524 559 531 541 11 FTSAICSVVRR 451 A*7401 77 1.69 130 14 524 559 532 541 10 TSAICSVVRR 452 A*3101 37 1.69 62 14 524 559 532 541 10 TSAICSVVRR 452 A*6801 99 1.69 167 14 524 559 533 541 9 SAICSVVRR 453 A*3101 6 1.69 11 14 524 559 533 541 9 SAICSVVRR 453 A*3303 63 1.69 107 14 524 559 533 541 9 SAICSVVRR 453 A*6801 85 1.69 144 14 524 559 533 541 9 SAICSVVRR 453 A*7401 46 1.69 78 14 524 559 534 541 8 AICSVVRR 454 A*3101 56 1.69 94 14 524 559 534 541 8 AICSVVRR 454 A*7401 84 1.69 142 14 524 559 533 543 11 SAICSVVRRAF 455 A*2501 10 1.06 11 14 524 559 533 543 11 SAICSVVRRAF 455 B*0702 12 1.06 12 14 524 559 533 543 11 SAICSVVRRAF 455 B*1501 78 1.06 83 14 524 559 533 543 11 SAICSVVRRAF 455 B*1502 94 1.06 100 14 524 559 533 543 11 SAICSVVRRAF 455 B*1525 88 1.06 94 14 524 559 533 543 11 SAICSVVRRAF 455 B*3501 71 1.06 75 14 524 559 533 543 11 SAICSVVRRAF 455 B*3503 31 1.06 33 14 524 559 533 543 11 SAICSVVRRAF 455 B*4601 90 1.06 96 14 524 559 536 543 8 CSVVRRAF 456 B*1502 30 1.06 31 14 524 559 536 543 8 CSVVRRAF 456 B*1525 3 1.06 4 14 524 559 536 543 8 CSVVRRAF 456 B*4601 36 1.06 38 14 524 559 536 545 10 CSVVRRAFPH 457 B*5801 8 0.14 1 14 524 559 538 545 8 VVRRAFPH 458 A*3001 10 0.14 1 14 524 559 537 546 10 SVVRRAFPHC 459 A*3001 28 0.21 6 14 524 559 537 547 11 SVVRRAFPHCL 460 B*0801 71 1.96 140 14 524 559 539 547 9 VRRAFPHCL 461 B*1402 28 1.96 56 14 524 559 539 547 9 VRRAFPHCL 461 B*2702 51 1.96 99 14 524 559 539 547 9 VRRAFPHCL 461 B*2705 3 1.96 6 14 524 559 540 547 8 RRAFPHCL 462 B*1402 47 1.96 93 14 524 559 540 547 8 RRAFPHCL 462 B*2702 96 1.96 189 14 524 559 540 547 8 RRAFPHCL 462 B*2705 93 1.96 182 14 524 559 540 547 8 RRAFPHCL 462 B*3901 9 1.96 18 14 524 559 540 547 8 RRAFPHCL 462 B*4801 6 1.96 11 14 524 559 538 548 11 VVRRAFPHCLA 463 A*3001 86 1.06 91 14 524 559 540 548 9 RRAFPHCLA 464 B*2702 45 1.06 47 14 524 559 540 548 9 RRAFPHCLA 464 B*2705 39 1.06 41 14 524 559 541 548 8 RAFPHCLA 465 A*3001 68 1.06 72 14 524 559 540 549 10 RRAFPHCLAF 466 B*2702 95 1.82 173 14 524 559 540 549 10 RRAFPHCLAF 466 B*2705 91 1.82 165 14 524 559 541 549 9 RAFPHCLAF 467 A*3201 73 1.82 132 14 524 559 541 549 9 RAFPHCLAF 467 B*1301 79 1.82 143 14 524 559 541 549 9 RAFPHCLAF 467 B*1402 66 1.82 119 14 524 559 541 549 9 RAFPHCLAF 467 B*1501 84 1.82 153 14 524 559 541 549 9 RAFPHCLAF 467 B*3501 68 1.82 124 14 524 559 541 549 9 RAFPHCLAF 467 B*4601 97 1.82 176 14 524 559 541 549 9 RAFPHCLAF 467 B*5201 75 1.82 135 14 524 559 541 549 9 RAFPHCLAF 467 B*5701 59 1.82 107 14 524 559 541 549 9 RAFPHCLAF 467 B*5801 81 1.82 148 14 524 559 542 549 8 AFPHCLAF 468 A*2301 71 1.82 128 14 524 559 542 549 8 AFPHCLAF 468 A*2402 70 1.82 128 14 524 559 543 550 8 FPHCLAFS 469 B*3501 67 0.25 17 14 524 559 543 550 8 FPHCLAFS 469 B*5501 17 0.25 4 14 524 559 543 550 8 FPHCLAFS 469 B*5601 56 0.25 14 14 524 559 541 551 11 RAFPHCLAFSY 470 A*0301 77 1.93 149 14 524 559 541 551 11 RAFPHCLAFSY 470 A*3201 94 1.93 182 14 524 559 541 551 11 RAFPHCLAFSY 470 B*1301 66 1.93 128 14 524 559 541 551 11 RAFPHCLAFSY 470 B*1501 91 1.93 175 14 524 559 541 551 11 RAFPHCLAFSY 470 B*1502 93 1.93 179 14 524 559 541 551 11 RAFPHCLAFSY 470 B*1525 95 1.93 183 14 524 559 541 551 11 RAFPHCLAFSY 470 B*5701 89 1.93 173 14 524 559 541 551 11 RAFPHCLAFSY 470 B*5802 86 1.93 165 14 524 559 542 551 10 AFPHCLAFSY 471 A*2902 94 1.93 181 14 524 559 543 551 9 FPHCLAFSY 472 B*3501 97 1.93 188 14 524 559 543 551 9 FPHCLAFSY 472 B*3503 91 1.93 175 14 524 559 543 551 9 FPHCLAFSY 472 B*5301 98 1.93 190 14 524 559 543 551 9 FPHCLAFSY 472 B*5501 83 1.93 160 14 524 559 542 552 11 AFPHCLAFSYM 473 A*2402 4 1.02 4 14 524 559 543 552 10 FPHCLAFSYM 474 B*0702 64 1.02 65 14 524 559 543 552 10 FPHCLAFSYM 474 B*1402 90 1.02 92 14 524 559 543 552 10 FPHCLAFSYM 474 B*3501 96 1.02 98 14 524 559 543 552 10 FPHCLAFSYM 474 B*3503 99 1.02 100 14 524 559 543 552 10 FPHCLAFSYM 474 B*3901 68 1.02 69 14 524 559 543 552 10 FPHCLAFSYM 474 B*5101 98 1.02 100 14 524 559 543 552 10 FPHCLAFSYM 474 B*5301 97 1.02 98 14 524 559 543 552 10 FPHCLAFSYM 474 B*5501 97 1.02 98 14 524 559 543 552 10 FPHCLAFSYM 474 B*5601 87 1.02 89 14 524 559 545 555 11 HCLAFSYMDDV 475 A*0201 73 0.60 44 14 524 559 547 555 9 LAFSYMDDV 476 B*5101 20 0.60 12 14 524 559 547 556 10 LAFSYMDDVV 477 B*5201 51 0.34 17 14 524 559 549 556 8 FSYMDDVV 478 B*4601 34 0.34 12 14 524 559 549 556 8 FSYMDDVV 478 B*5101 23 0.34 8 14 524 559 549 556 8 FSYMDDVV 478 B*5201 39 0.34 13 14 524 559 547 557 11 LAFSYMDDVVL 479 B*3503 11 1.21 13 14 524 559 547 557 11 LAFSYMDDVVL 479 B*3801 29 1.21 35 14 524 559 547 557 11 LAFSYMDDVVL 479 B*3901 19 1.21 24 14 524 559 547 557 11 LAFSYMDDVVL 479 B*4801 23 1.21 28 14 524 559 549 557 9 FSYMDDVVL 480 B*3901 25 1.21 30 14 524 559 549 557 9 FSYMDDVVL 480 B*4601 62 1.21 76 14 524 559 550 557 8 SYMDDVVL 481 A*2301 38 1.21 46 14 524 559 550 557 8 SYMDDVVL 481 A*2402 47 1.21 57 14 524 559 551 559 9 YMDDVVLGA 482 A*0101 66 1.49 98 14 524 559 551 559 9 YMDDVVLGA 482 A*0201 100 1.49 149 14 524 559 551 559 9 YMDDVVLGA 482 A*0206 71 1.49 105 14 524 559 552 559 8 MDDVVLGA 483 A*6802 34 1.49 50 14 524 559 Cumulative Class I-BCI score: 12015 526 533 8 FLLAQFTS 435 A*0201 42 0.76 32 15 526 559 524 534 11 SPFLLAQFTSA 436 B*0702 46 0.92 43 15 526 559 524 534 11 SPFLLAQFTSA 436 B*3503 3 0.92 2 15 526 559 524 534 11 SPFLLAQFTSA 436 B*5101 25 0.92 23 15 526 559 524 534 11 SPFLLAQFTSA 436 B*5501 98 0.92 90 15 526 559 524 534 11 SPFLLAQFTSA 436 B*5601 95 0.92 88 15 526 559 526 534 9 FLLAQFTSA 437 A*0201 84 0.92 78 15 526 559 526 534 9 FLLAQFTSA 437 A*0206 98 0.92 91 15 526 559 526 534 9 FLLAQFTSA 437 B*0801 78 0.92 72 15 526 559 526 535 10 FLLAQFTSAI 438 A*0201 76 0.94 71 15 526 559 526 535 10 FLLAQFTSAI 438 A*0206 79 0.94 75 15 526 559 526 535 10 FLLAQFTSAI 438 B*1302 11 0.94 11 15 526 559 526 535 10 FLLAQFTSAI 438 B*3801 47 0.94 44 15 526 559 526 535 10 FLLAQFTSAI 438 B*4601 11 0.94 11 15 526 559 526 535 10 FLLAQFTSAI 438 B*5201 14 0.94 13 15 526 559 527 535 9 LLAQFTSAI 439 A*3201 3 0.94 3 15 526 559 527 535 9 LLAQFTSAI 439 B*1525 17 0.94 16 15 526 559 527 535 9 LLAQFTSAI 439 B*5501 19 0.94 18 15 526 559 528 535 8 LAQFTSAI 440 B*5101 62 0.94 58 15 526 559 528 535 8 LAQFTSAI 440 B*5201 76 0.94 72 15 526 559 528 535 8 LAQFTSAI 440 B*5301 5 0.94 5 15 526 559 527 537 11 LLAQFTSAICS 441 A*6802 22 0.41 9 15 526 559 528 538 11 LAQFTSAICSV 442 B*5101 13 1.40 19 15 526 559 528 538 11 LAQFTSAICSV 442 B*5201 12 1.40 16 15 526 559 529 538 10 AQFTSAICSV 443 A*0201 55 1.40 77 15 526 559 529 538 10 AQFTSAICSV 443 A*0206 85 1.40 119 15 526 559 529 538 10 AQFTSAICSV 443 B*1301 83 1.40 116 15 526 559 529 538 10 AQFTSAICSV 443 B*1302 46 1.40 65 15 526 559 529 538 10 AQFTSAICSV 443 B*3701 14 1.40 20 15 526 559 529 538 10 AQFTSAICSV 443 B*3901 10 1.40 15 15 526 559 529 538 10 AQFTSAICSV 443 B*4801 77 1.40 108 15 526 559 529 538 10 AQFTSAICSV 443 B*4901 30 1.40 43 15 526 559 529 538 10 AQFTSAICSV 443 B*5001 64 1.40 90 15 526 559 529 538 10 AQFTSAICSV 443 B*5201 82 1.40 115 15 526 559 531 538 8 FTSAICSV 444 A*2501 82 1.40 114 15 526 559 531 538 8 FTSAICSV 444 A*2601 49 1.40 68 15 526 559 529 539 11 AQFTSAICSVV 445 B*1301 75 1.34 100 15 526 559 529 539 11 AQFTSAICSVV 445 B*1302 41 1.34 55 15 526 559 529 539 11 AQFTSAICSVV 445 B*4002 20 1.34 27 15 526 559 529 539 11 AQFTSAICSVV 445 B*4801 62 1.34 83 15 526 559 529 539 11 AQFTSAICSVV 445 B*4901 26 1.34 35 15 526 559 529 539 11 AQFTSAICSVV 445 B*5001 60 1.34 81 15 526 559 529 539 11 AQFTSAICSVV 445 B*5201 53 1.34 71 15 526 559 531 539 9 FTSAICSVV 446 A*6802 49 1.34 65 15 526 559 531 539 9 FTSAICSVV 446 B*4601 31 1.34 42 15 526 559 531 539 9 FTSAICSVV 446 B*5201 2 1.34 3 15 526 559 531 539 9 FTSAICSVV 446 B*5601 4 1.34 5 15 526 559 530 540 11 QFTSAICSVVR 447 A*3303 30 1.19 35 15 526 559 531 540 10 FTSAICSVVR 448 A*3101 38 1.19 45 15 526 559 531 540 10 FTSAICSVVR 448 A*3303 92 1.19 109 15 526 559 531 540 10 FTSAICSVVR 448 A*6801 100 1.19 119 15 526 559 531 540 10 FTSAICSVVR 448 A*7401 68 1.19 81 15 526 559 531 540 10 FTSAICSVVR 448 B*5701 23 1.19 27 15 526 559 532 540 9 TSAICSVVR 449 A*6801 82 1.19 98 15 526 559 533 540 8 SAICSVVR 450 A*3101 11 1.19 14 15 526 559 533 540 8 SAICSVVR 450 A*3303 39 1.19 47 15 526 559 533 540 8 SAICSVVR 450 A*6801 81 1.19 96 15 526 559 531 541 11 FTSAICSVVRR 451 A*1101 2 1.69 4 15 526 559 531 541 11 FTSAICSVVRR 451 A*3101 32 1.69 54 15 526 559 531 541 11 FTSAICSVVRR 451 A*3303 96 1.69 162 15 526 559 531 541 11 FTSAICSVVRR 451 A*7401 77 1.69 130 15 526 559 532 541 10 TSAICSVVRR 452 A*3101 37 1.69 62 15 526 559 532 541 10 TSAICSVVRR 452 A*6801 99 1.69 167 15 526 559 533 541 9 SAICSVVRR 453 A*3101 6 1.69 11 15 526 559 533 541 9 SAICSVVRR 453 A*3303 63 1.69 107 15 526 559 533 541 9 SAICSVVRR 453 A*6801 85 1.69 144 15 526 559 533 541 9 SAICSVVRR 453 A*7401 46 1.69 78 15 526 559 534 541 8 AICSVVRR 454 A*3101 56 1.69 94 15 526 559 534 541 8 AICSVVRR 454 A*7401 84 1.69 142 15 526 559 533 543 11 SAICSVVRRAF 455 A*2501 10 1.06 11 15 526 559 533 543 11 SAICSVVRRAF 455 B*0702 12 1.06 12 15 526 559 533 543 11 SAICSVVRRAF 455 B*1501 78 1.06 83 15 526 559 533 543 11 SAICSVVRRAF 455 B*1502 94 1.06 100 15 526 559 533 543 11 SAICSVVRRAF 455 B*1525 88 1.06 94 15 526 559 533 543 11 SAICSVVRRAF 455 B*3501 71 1.06 75 15 526 559 533 543 11 SAICSVVRRAF 455 B*3503 31 1.06 33 15 526 559 533 543 11 SAICSVVRRAF 455 B*4601 90 1.06 96 15 526 559 536 543 8 CSVVRRAF 456 B*1502 30 1.06 31 15 526 559 536 543 8 CSVVRRAF 456 B*1525 3 1.06 4 15 526 559 536 543 8 CSVVRRAF 456 B*4601 36 1.06 38 15 526 559 536 545 10 CSVVRRAFPH 457 B*5801 8 0.14 1 15 526 559 538 545 8 VVRRAFPH 458 A*3001 10 0.14 1 15 526 559 537 546 10 SVVRRAFPHC 459 A*3001 28 0.21 6 15 526 559 537 547 11 SVVRRAFPHCL 460 B*0801 71 1.96 140 15 526 559 539 547 9 VRRAFPHCL 461 B*1402 28 1.96 56 15 526 559 539 547 9 VRRAFPHCL 461 B*2702 51 1.96 99 15 526 559 539 547 9 VRRAFPHCL 461 B*2705 3 1.96 6 15 526 559 540 547 8 RRAFPHCL 462 B*1402 47 1.96 93 15 526 559 540 547 8 RRAFPHCL 462 B*2702 96 1.96 189 15 526 559 540 547 8 RRAFPHCL 462 B*2705 93 1.96 182 15 526 559 540 547 8 RRAFPHCL 462 B*3901 9 1.96 18 15 526 559 540 547 8 RRAFPHCL 462 B*4801 6 1.96 11 15 526 559 538 548 11 VVRRAFPHCLA 463 A*3001 86 1.06 91 15 526 559 540 548 9 RRAFPHCLA 464 B*2702 45 1.06 47 15 526 559 540 548 9 RRAFPHCLA 464 B*2705 39 1.06 41 15 526 559 541 548 8 RAFPHCLA 465 A*3001 68 1.06 72 15 526 559 540 549 10 RRAFPHCLAF 466 B*2702 95 1.82 173 15 526 559 540 549 10 RRAFPHCLAF 466 B*2705 91 1.82 165 15 526 559 541 549 9 RAFPHCLAF 467 A*3201 73 1.82 132 15 526 559 541 549 9 RAFPHCLAF 467 B*1301 79 1.82 143 15 526 559 541 549 9 RAFPHCLAF 467 B*1402 66 1.82 119 15 526 559 541 549 9 RAFPHCLAF 467 B*1501 84 1.82 153 15 526 559 541 549 9 RAFPHCLAF 467 B*3501 68 1.82 124 15 526 559 541 549 9 RAFPHCLAF 467 B*4601 97 1.82 176 15 526 559 541 549 9 RAFPHCLAF 467 B*5201 75 1.82 135 15 526 559 541 549 9 RAFPHCLAF 467 B*5701 59 1.82 107 15 526 559 541 549 9 RAFPHCLAF 467 B*5801 81 1.82 148 15 526 559 542 549 8 AFPHCLAF 468 A*2301 71 1.82 128 15 526 559 542 549 8 AFPHCLAF 468 A*2402 70 1.82 128 15 526 559 543 550 8 FPHCLAFS 469 B*3501 67 0.25 17 15 526 559 543 550 8 FPHCLAFS 469 B*5501 17 0.25 4 15 526 559 543 550 8 FPHCLAFS 469 B*5601 56 0.25 14 15 526 559 541 551 11 RAFPHCLAFSY 470 A*0301 77 1.93 149 15 526 559 541 551 11 RAFPHCLAFSY 470 A*3201 94 1.93 182 15 526 559 541 551 11 RAFPHCLAFSY 470 B*1301 66 1.93 128 15 526 559 541 551 11 RAFPHCLAFSY 470 B*1501 91 1.93 175 15 526 559 541 551 11 RAFPHCLAFSY 470 B*1502 93 1.93 179 15 526 559 541 551 11 RAFPHCLAFSY 470 B*1525 95 1.93 183 15 526 559 541 551 11 RAFPHCLAFSY 470 B*5701 89 1.93 173 15 526 559 541 551 11 RAFPHCLAFSY 470 B*5802 86 1.93 165 15 526 559 542 551 10 AFPHCLAFSY 471 A*2902 94 1.93 181 15 526 559 543 551 9 FPHCLAFSY 472 B*3501 97 1.93 188 15 526 559 543 551 9 FPHCLAFSY 472 B*3503 91 1.93 175 15 526 559 543 551 9 FPHCLAFSY 472 B*5301 98 1.93 190 15 526 559 543 551 9 FPHCLAFSY 472 B*5501 83 1.93 160 15 526 559 542 552 11 AFPHCLAFSYM 473 A*2402 4 1.02 4 15 526 559 543 552 10 FPHCLAFSYM 474 B*0702 64 1.02 65 15 526 559 543 552 10 FPHCLAFSYM 474 B*1402 90 1.02 92 15 526 559 543 552 10 FPHCLAFSYM 474 B*3501 96 1.02 98 15 526 559 543 552 10 FPHCLAFSYM 474 B*3503 99 1.02 100 15 526 559 543 552 10 FPHCLAFSYM 474 B*3901 68 1.02 69 15 526 559 543 552 10 FPHCLAFSYM 474 B*5101 98 1.02 100 15 526 559 543 552 10 FPHCLAFSYM 474 B*5301 97 1.02 98 15 526 559 543 552 10 FPHCLAFSYM 474 B*5501 97 1.02 98 15 526 559 543 552 10 FPHCLAFSYM 474 B*5601 87 1.02 89 15 526 559 545 555 11 HCLAFSYMDDV 475 A*0201 73 0.60 44 15 526 559 547 555 9 LAFSYMDDV 476 B*5101 20 0.60 12 15 526 559 547 556 10 LAFSYMDDVV 477 B*5201 51 0.34 17 15 526 559 549 556 8 FSYMDDVV 478 B*4601 34 0.34 12 15 526 559 549 556 8 FSYMDDVV 478 B*5101 23 0.34 8 15 526 559 549 556 8 FSYMDDVV 478 B*5201 39 0.34 13 15 526 559 547 557 11 LAFSYMDDVVL 479 B*3503 11 1.21 13 15 526 559 547 557 11 LAFSYMDDVVL 479 B*3801 29 1.21 35 15 526 559 547 557 11 LAFSYMDDVVL 479 B*3901 19 1.21 24 15 526 559 547 557 11 LAFSYMDDVVL 479 B*4801 23 1.21 28 15 526 559 549 557 9 FSYMDDVVL 480 B*3901 25 1.21 30 15 526 559 549 557 9 FSYMDDVVL 480 B*4601 62 1.21 76 15 526 559 550 557 8 SYMDDVVL 481 A*2301 38 1.21 46 15 526 559 550 557 8 SYMDDVVL 481 A*2402 47 1.21 57 15 526 559 551 559 9 YMDDVVLGA 482 A*0101 66 1.49 98 15 526 559 551 559 9 YMDDVVLGA 482 A*0201 100 1.49 149 15 526 559 551 559 9 YMDDVVLGA 482 A*0206 71 1.49 105 15 526 559 552 559 8 MDDVVLGA 483 A*6802 34 1.49 50 15 526 559 Cumulative Class I-BCI score: 11658 565 572 8 RESLYTAV 486 B*1301 93 1.67 155 16 565 598 565 572 8 RESLYTAV 486 B*1302 31 1.67 52 16 565 598 565 572 8 RESLYTAV 486 B*3701 81 1.67 135 16 565 598 565 572 8 RESLYTAV 486 B*4001 91 1.67 153 16 565 598 565 572 8 RESLYTAV 486 B*4002 90 1.67 151 16 565 598 565 572 8 RESLYTAV 486 B*4402 65 1.67 109 16 565 598 565 572 8 RESLYTAV 486 B*4403 52 1.67 87 16 565 598 565 572 8 RESLYTAV 486 B*4801 44 1.67 74 16 565 598 565 572 8 RESLYTAV 486 B*4901 87 1.67 145 16 565 598 565 572 8 RESLYTAV 486 B*5001 88 1.67 147 16 565 598 565 573 9 RESLYTAVT 487 B*4002 40 1.11 45 16 565 598 565 573 9 RESLYTAVT 487 B*5001 56 1.11 62 16 565 598 565 574 10 RESLYTAVTN 488 B*4002 35 0.69 24 16 565 598 565 575 11 RESLYTAVTNF 489 B*1301 73 1.85 136 16 565 598 565 575 11 RESLYTAVTNF 489 B*1801 81 1.85 150 16 565 598 565 575 11 RESLYTAVTNF 489 B*4001 78 1.85 145 16 565 598 565 575 11 RESLYTAVTNF 489 B*4002 75 1.85 139 16 565 598 565 575 11 RESLYTAVTNF 489 B*4402 96 1.85 178 16 565 598 565 575 11 RESLYTAVTNF 489 B*4403 92 1.85 170 16 565 598 565 575 11 RESLYTAVTNF 489 B*4901 70 1.85 129 16 565 598 565 575 11 RESLYTAVTNF 489 B*5001 68 1.85 126 16 565 598 566 575 10 ESLYTAVTNF 490 A*2601 95 1.85 176 16 565 598 567 575 9 SLYTAVTNF 491 B*1501 64 1.85 119 16 565 598 567 575 9 SLYTAVTNF 491 B*1525 86 1.85 160 16 565 598 568 575 8 LYTAVTNF 492 A*2301 90 1.85 166 16 565 598 568 575 8 LYTAVTNF 492 A*2402 91 1.85 169 16 565 598 567 576 10 SLYTAVTNFL 493 A*0201 64 1.69 109 16 565 598 568 576 9 LYTAVTNFL 494 A*2301 16 1.69 26 16 565 598 568 576 9 LYTAVTNFL 494 A*2402 53 1.69 89 16 565 598 569 576 8 YTAVTNFL 495 A*0101 2 1.69 3 16 565 598 569 576 8 YTAVTNFL 495 A*2501 71 1.69 121 16 565 598 569 576 8 YTAVTNFL 495 A*2601 59 1.69 100 16 565 598 569 576 8 YTAVTNFL 495 B*4601 80 1.69 136 16 565 598 567 577 11 SLYTAVTNFLL 496 A*3201 48 1.86 90 16 565 598 568 577 10 LYTAVTNFLL 497 A*2301 60 1.86 112 16 565 598 568 577 10 LYTAVTNFLL 497 A*2402 67 1.86 124 16 565 598 568 577 10 LYTAVTNFLL 497 B*3801 8 1.86 15 16 565 598 569 577 9 YTAVTNFLL 498 A*0101 70 1.86 130 16 565 598 569 577 9 YTAVTNFLL 498 A*6802 28 1.86 52 16 565 598 569 577 9 YTAVTNFLL 498 B*5801 41 1.86 75 16 565 598 569 579 11 YTAVTNFLLSL 499 A*0101 58 1.91 112 16 565 598 569 579 11 YTAVTNFLLSL 499 A*2501 69 1.91 132 16 565 598 569 579 11 YTAVTNFLLSL 499 A*2601 56 1.91 108 16 565 598 569 579 11 YTAVTNFLLSL 499 B*3801 43 1.91 82 16 565 598 569 579 11 YTAVTNFLLSL 499 B*4601 89 1.91 169 16 565 598 569 579 11 YTAVTNFLLSL 499 B*5801 14 1.91 26 16 565 598 572 579 8 VTNFLLSL 500 A*3201 26 1.91 49 16 565 598 572 579 8 VTNFLLSL 500 B*0702 23 1.91 44 16 565 598 571 581 11 AVTNFLLSLGI 501 A*3201 9 1.49 14 16 565 598 573 581 9 TNFLLSLGI 502 B*5201 31 1.49 47 16 565 598 575 583 9 FLLSLGIHL 503 A*0201 82 1.27 104 16 565 598 575 583 9 FLLSLGIHL 503 A*0206 46 1.27 58 16 565 598 576 583 8 LLSLGIHL 504 B*0702 90 1.27 114 16 565 598 578 585 8 SLGIHLNP 505 A*0201 98 0.14 14 16 565 598 576 586 11 LLSLGIHLNPN 506 A*0206 75 0.09 7 16 565 598 577 587 11 LSLGIHLNPNK 507 A*0301 10 0.12 1 16 565 598 577 587 11 LSLGIHLNPNK 507 A*1101 50 0.12 6 16 565 598 578 587 10 SLGIHLNPNK 508 A*0301 30 0.12 3 16 565 598 578 587 10 SLGIHLNPNK 508 A*1101 24 0.12 3 16 565 598 580 587 8 GIHLNPNK 509 A*0301 26 0.12 3 16 565 598 580 587 8 GIHLNPNK 509 A*1101 17 0.12 2 16 565 598 582 589 8 HLNPNKTK 510 A*0301 51 1.61 82 16 565 598 582 590 9 HLNPNKTKR 511 A*3101 85 1.52 129 16 565 598 582 590 9 HLNPNKTKR 511 A*3303 54 1.52 81 16 565 598 582 590 9 HLNPNKTKR 511 A*7401 20 1.52 30 16 565 598 584 591 8 NPNKTKRW 512 B*5301 46 1.80 83 16 565 598 585 594 10 PNKTKRWGYS 513 A*3201 55 0.53 29 16 565 598 587 594 8 KTKRWGYS 514 A*3001 67 0.53 36 16 565 598 586 595 10 NKTKRWGYSL 515 B*1402 46 1.81 84 16 565 598 587 595 9 KTKRWGYSL 516 A*3001 64 1.81 116 16 565 598 587 595 9 KTKRWGYSL 516 A*3201 85 1.81 154 16 565 598 587 595 9 KTKRWGYSL 516 B*5701 50 1.81 91 16 565 598 587 595 9 KTKRWGYSL 516 B*5802 52 1.81 94 16 565 598 588 595 8 TKRWGYSL 517 B*1402 56 1.81 101 16 565 598 589 596 8 KRWGYSLN 518 B*2702 42 0.19 8 16 565 598 589 596 8 KRWGYSLN 518 B*2705 75 0.19 14 16 565 598 587 597 11 KTKRWGYSLNF 519 A*2402 2 1.95 3 16 565 598 587 597 11 KTKRWGYSLNF 519 A*3001 41 1.95 80 16 565 598 587 597 11 KTKRWGYSLNF 519 A*3002 41 1.95 80 16 565 598 587 597 11 KTKRWGYSLNF 519 A*3201 91 1.95 177 16 565 598 587 597 11 KTKRWGYSLNF 519 B*5701 77 1.95 150 16 565 598 587 597 11 KTKRWGYSLNF 519 B*5801 44 1.95 86 16 565 598 587 597 11 KTKRWGYSLNF 519 B*5802 81 1.95 158 16 565 598 589 597 9 KRWGYSLNF 520 A*3201 12 1.95 24 16 565 598 589 597 9 KRWGYSLNF 520 B*2705 96 1.95 186 16 565 598 590 597 8 RWGYSLNF 521 A*2301 88 1.95 171 16 565 598 590 597 8 RWGYSLNF 521 A*2402 89 1.95 174 16 565 598 590 597 8 RWGYSLNF 521 B*2705 63 1.95 122 16 565 598 589 598 10 KRWGYSLNFM 522 B*2702 100 0.84 84 16 565 598 589 598 10 KRWGYSLNFM 522 B*2705 43 0.84 36 16 565 598 589 598 10 KRWGYSLNFM 522 B*3901 5 0.84 4 16 565 598 590 598 9 RWGYSLNFM 523 A*2402 7 0.84 6 16 565 598 Cumulative Class I-BCI score: 8255 585 594 10 PNKTKRWGYS 513 A*3201 55 0.53 29 17 584 617 587 594 8 KTKRWGYS 514 A*3001 67 0.53 36 17 584 617 586 595 10 NKTKRWGYSL 515 B*1402 46 1.81 84 17 584 617 587 595 9 KTKRWGYSL 516 A*3001 64 1.81 116 17 584 617 587 595 9 KTKRWGYSL 516 A*3201 85 1.81 154 17 584 617 587 595 9 KTKRWGYSL 516 B*5701 50 1.81 91 17 584 617 587 595 9 KTKRWGYSL 516 B*5802 52 1.81 94 17 584 617 588 595 8 TKRWGYSL 517 B*1402 56 1.81 101 17 584 617 589 596 8 KRWGYSLN 518 B*2702 42 0.19 8 17 584 617 589 596 8 KRWGYSLN 518 B*2705 75 0.19 14 17 584 617 587 597 11 KTKRWGYSLNF 519 A*2402 2 1.95 3 17 584 617 587 597 11 KTKRWGYSLNF 519 A*3001 41 1.95 80 17 584 617 587 597 11 KTKRWGYSLNF 519 A*3002 41 1.95 80 17 584 617 587 597 11 KTKRWGYSLNF 519 A*3201 91 1.95 177 17 584 617 587 597 11 KTKRWGYSLNF 519 B*5701 77 1.95 150 17 584 617 587 597 11 KTKRWGYSLNF 519 B*5801 44 1.95 86 17 584 617 587 597 11 KTKRWGYSLNF 519 B*5802 81 1.95 158 17 584 617 589 597 9 KRWGYSLNF 520 A*3201 12 1.95 24 17 584 617 589 597 9 KRWGYSLNF 520 B*2705 96 1.95 186 17 584 617 590 597 8 RWGYSLNF 521 A*2301 88 1.95 171 17 584 617 590 597 8 RWGYSLNF 521 A*2402 89 1.95 174 17 584 617 590 597 8 RWGYSLNF 521 B*2705 63 1.95 122 17 584 617 589 598 10 KRWGYSLNFM 522 B*2702 100 0.84 84 17 584 617 589 598 10 KRWGYSLNFM 522 B*2705 43 0.84 36 17 584 617 589 598 10 KRWGYSLNFM 522 B*3901 5 0.84 4 17 584 617 590 598 9 RWGYSLNFM 523 A*2402 7 0.84 6 17 584 617 589 599 11 KRWGYSLNFMG 524 B*2702 57 0.64 36 17 584 617 589 599 11 KRWGYSLNFMG 524 B*2705 24 0.64 15 17 584 617 590 600 11 RWGYSLNFMGY 525 A*3002 82 1.89 155 17 584 617 592 600 9 GYSLNFMGY 526 A*2902 73 1.89 138 17 584 617 593 600 8 YSLNFMGY 527 A*0101 87 1.89 164 17 584 617 593 600 8 YSLNFMGY 527 A*2501 88 1.89 166 17 584 617 593 600 8 YSLNFMGY 527 A*2601 87 1.89 165 17 584 617 593 600 8 YSLNFMGY 527 A*2902 100 1.89 189 17 584 617 593 600 8 YSLNFMGY 527 A*3002 86 1.89 163 17 584 617 593 600 8 YSLNFMGY 527 B*1501 42 1.89 80 17 584 617 593 600 8 YSLNFMGY 527 B*1502 48 1.89 91 17 584 617 593 600 8 YSLNFMGY 527 B*1525 37 1.89 71 17 584 617 593 600 8 YSLNFMGY 527 B*4601 79 1.89 149 17 584 617 593 600 8 YSLNFMGY 527 B*5801 27 1.89 51 17 584 617 593 600 8 YSLNFMGY 527 B*5802 25 1.89 47 17 584 617 591 601 11 WGYSLNFMGYI 528 B*1302 25 0.91 23 17 584 617 591 601 11 WGYSLNFMGYI 528 B*5201 67 0.91 60 17 584 617 593 601 9 YSLNFMGYI 529 A*2501 76 0.91 68 17 584 617 593 601 9 YSLNFMGYI 529 B*4601 30 0.91 27 17 584 617 593 601 9 YSLNFMGYI 529 B*5201 49 0.91 44 17 584 617 593 601 9 YSLNFMGYI 529 B*5802 78 0.91 71 17 584 617 594 601 8 SLNFMGYI 530 A*3201 39 0.91 36 17 584 617 592 602 11 GYSLNFMGYII 531 A*2301 62 0.67 42 17 584 617 592 602 11 GYSLNFMGYII 531 A*2402 68 0.67 46 17 584 617 593 602 10 YSLNFMGYII 532 A*0206 52 0.67 35 17 584 617 593 602 10 YSLNFMGYII 532 B*1301 62 0.67 42 17 584 617 593 602 10 YSLNFMGYII 532 B*1302 39 0.67 27 17 584 617 593 602 10 YSLNFMGYII 532 B*3801 20 0.67 14 17 584 617 593 602 10 YSLNFMGYII 532 B*5201 92 0.67 62 17 584 617 593 602 10 YSLNFMGYII 532 B*5802 4 0.67 3 17 584 617 594 602 9 SLNFmGyII 533 A*3201 71 0.67 48 17 584 617 595 602 8 LNFMGYII 534 B*1302 30 0.67 20 17 584 617 595 602 8 LNFMGYII 534 B*5101 7 0.67 4 17 584 617 595 602 8 LNFMGYII 534 B*5201 90 0.67 61 17 584 617 597 604 8 FMGYIIGS 535 A*0201 36 0.52 19 17 584 617 595 605 11 LNFMGYIIGSW 536 B*5701 5 1.77 8 17 584 617 596 605 10 NFMGYIIGSW 537 A*2301 50 1.77 88 17 584 617 596 605 10 NFMGYIIGSW 537 B*4402 50 1.77 88 17 584 617 597 605 9 FMGYIIGSW 538 B*4601 52 1.77 93 17 584 617 598 605 8 MGYIIGSW 539 A*6802 25 1.77 44 17 584 617 598 605 8 MGYIIGSW 539 B*5201 29 1.77 52 17 584 617 598 605 8 MGYIIGSW 539 B*5301 56 1.77 99 17 584 617 598 605 8 MGYIIGSW 539 B*5701 85 1.77 150 17 584 617 598 605 8 MGYIIGSW 539 B*5801 78 1.77 138 17 584 617 598 605 8 MGYIIGSW 539 B*5802 80 1.77 141 17 584 617 598 608 11 MGYIIGSWGTL 540 B*1402 33 1.71 57 17 584 617 599 608 10 GYIIGSWGTL 541 A*3201 83 1.71 142 17 584 617 600 608 9 YIIGSWGTL 542 A*0206 2 1.71 4 17 584 617 600 608 9 YIIGSWGTL 542 A*2501 92 1.71 157 17 584 617 600 608 9 YIIGSWGTL 542 A*2601 28 1.71 48 17 584 617 600 608 9 YIIGSWGTL 542 B*1502 67 1.71 114 17 584 617 607 614 8 TLPQDHIV 543 A*0201 4 0.56 2 17 584 617 606 616 11 GTLPQDHIVQK 544 A*0301 8 1.05 9 17 584 617 606 616 11 GTLPQDHIVQK 544 A*1101 63 1.05 66 17 584 617 608 617 10 LPQDHIVQKI 545 B*5101 82 1.83 150 17 584 617 608 617 10 LPQDHIVQKI 545 B*5301 26 1.83 48 17 584 617 Cumulative BCI Class Iscore: 6396 653 660 8 YPALMPLY 548 A*0101 36 1.81 65 18 653 691 653 660 8 YPALMPLY 548 A*2601 21 1.81 37 18 653 691 653 660 8 YPALMPLY 548 A*2902 41 1.81 75 18 653 691 653 660 8 YPALMPLY 548 B*3501 95 1.81 171 18 653 691 653 660 8 YPALMPLY 548 B*3503 84 1.81 151 18 653 691 653 660 8 YPALMPLY 548 B*5101 38 1.81 69 18 653 691 653 660 8 YPALMPLY 548 B*5301 89 1.81 160 18 653 691 653 660 8 YPALMPLY 548 B*5501 28 1.81 50 18 653 691 653 660 8 YPALMPLY 548 B*5601 37 1.81 67 18 653 691 652 661 10 GYPALMPLYA 549 A*2402 40 1.43 58 18 653 691 653 661 9 YPALMPLYA 550 B*0702 9 1.43 12 18 653 691 653 661 9 YPALMPLYA 550 B*3503 59 1.43 85 18 653 691 653 661 9 YPALMPLYA 550 B*5101 27 1.43 38 18 653 691 653 661 9 YPALMPLYA 550 B*5501 94 1.43 135 18 653 691 653 661 9 YPALMPLYA 550 B*5601 100 1.43 143 18 653 691 653 662 10 YPALMPLYAC 551 B*0702 4 0.21 1 18 653 691 653 662 10 YPALMPLYAC 551 B*3501 72 0.21 15 18 653 691 653 662 10 YPALMPLYAC 551 B*3503 69 0.21 14 18 653 691 653 662 10 YPALMPLYAC 551 B*5301 54 0.21 11 18 653 691 653 662 10 YPALMPLYAC 551 B*5501 70 0.21 15 18 653 691 653 662 10 YPALMPLYAC 551 B*5601 86 0.21 18 18 653 691 655 662 8 ALMPLYAC 552 A*0201 11 0.21 2 18 653 691 653 663 11 YPALMPLYACI 553 B*0702 54 1.19 64 18 653 691 653 663 11 YPALMPLYACI 553 B*1402 40 1.19 48 18 653 691 653 663 11 YPALMPLYACI 553 B*3501 33 1.19 40 18 653 691 653 663 11 YPALMPLYACI 553 B*3503 82 1.19 98 18 653 691 653 663 11 YPALMPLYACI 553 B*5101 100 1.19 119 18 653 691 653 663 11 YPALMPLYACI 553 B*5201 27 1.19 33 18 653 691 653 663 11 YPALMPLYACI 553 B*5301 87 1.19 104 18 653 691 653 663 11 YPALMPLYACI 553 B*5501 69 1.19 82 18 653 691 653 663 11 YPALMPLYACI 553 B*5601 77 1.19 92 18 653 691 655 663 9 ALMPLYACI 554 A*0201 67 1.19 80 18 653 691 657 664 8 MPLYACIQ 555 B*5501 12 0.20 2 18 653 691 657 664 8 MPLYACIQ 555 B*5601 8 0.20 2 18 653 691 657 665 9 MPLYACIQA 556 B*3501 44 1.41 62 18 653 691 657 665 9 MPLYACIQA 556 B*3503 49 1.41 68 18 653 691 657 665 9 MPLYACIQA 556 B*5101 80 1.41 112 18 653 691 657 665 9 MPLYACIQA 556 B*5501 93 1.41 131 18 653 691 657 665 9 MPLYACIQA 556 B*5601 99 1.41 139 18 653 691 657 666 10 MPLYACIQAK 557 B*3501 43 1.01 43 18 653 691 657 666 10 MPLYACIQAK 557 B*5601 3 1.01 3 18 653 691 658 666 9 PLYACIQAK 558 A*0301 74 1.01 75 18 653 691 659 669 11 LYACIQAKQAF 559 A*2301 86 1.07 92 18 653 691 659 669 11 LYACIQAKQAF 559 A*2402 88 1.07 94 18 653 691 660 669 10 YACIQAKQAF 560 B*1502 26 1.07 28 18 653 691 663 671 9 IQAKQAFTF 561 A*2402 84 1.58 133 18 653 691 663 671 9 IQAKQAFTF 561 B*1301 61 1.58 96 18 653 691 663 671 9 IQAKQAFTF 561 B*1501 63 1.58 99 18 653 691 663 671 9 IQAKQAFTF 561 B*1525 71 1.58 112 18 653 691 664 671 8 QAKQAFTF 562 B*1501 8 1.58 12 18 653 691 664 671 8 QAKQAFTF 562 B*1502 37 1.58 59 18 653 691 664 671 8 QAKQAFTF 562 B*1525 14 1.58 21 18 653 691 664 671 8 QAKQAFTF 562 B*5802 3 1.58 5 18 653 691 666 675 10 KQAFTFSPTY 563 A*2902 27 1.81 49 18 653 691 666 675 10 KQAFTFSPTY 563 A*3002 30 1.81 53 18 653 691 666 675 10 KQAFTFSPTY 563 B*1501 89 1.81 161 18 653 691 666 675 10 KQAFTFSPTY 563 B*1502 63 1.81 114 18 653 691 666 675 10 KQAFTFSPTY 563 B*1525 85 1.81 153 18 653 691 666 675 10 KQAFTFSPTY 563 B*5001 32 1.81 58 18 653 691 667 675 9 QAFTFSPTY 564 A*2902 46 1.81 83 18 653 691 667 675 9 QAFTFSPTY 564 A*3002 58 1.81 104 18 653 691 667 675 9 QAFTFSPTY 564 B*1525 66 1.81 119 18 653 691 667 675 9 QAFTFSPTY 564 B*3501 73 1.81 133 18 653 691 667 675 9 QAFTFSPTY 564 B*5701 12 1.81 22 18 653 691 668 675 8 AFTFSPTY 565 A*2902 60 1.81 109 18 653 691 668 675 8 AFTFSPTY 565 A*3002 56 1.81 102 18 653 691 666 676 11 KQAFTFSPTYK 566 A*0301 100 1.78 178 18 653 691 666 676 11 KQAFTFSPTYK 566 A*1101 83 1.78 147 18 653 691 666 676 11 KQAFTFSPTYK 566 A*3001 49 1.78 87 18 653 691 666 676 11 KQAFTFSPTYK 566 A*7401 60 1.78 106 18 653 691 667 676 10 QAFTFSPTYK 567 A*0301 64 1.78 114 18 653 691 667 676 10 QAFTFSPTYK 567 A*1101 78 1.78 139 18 653 691 667 676 10 QAFTFSPTYK 567 A*6801 91 1.78 162 18 653 691 667 676 10 QAFTFSPTYK 567 A*7401 59 1.78 104 18 653 691 669 676 8 FTFSPTYK 568 A*0301 98 1.78 175 18 653 691 669 676 8 FTFSPTYK 568 A*1101 96 1.78 170 18 653 691 669 676 8 FTFSPTYK 568 A*3101 25 1.78 45 18 653 691 669 676 8 FTFSPTYK 568 A*3303 69 1.78 123 18 653 691 669 676 8 FTFSPTYK 568 A*7401 99 1.78 176 18 653 691 669 677 9 FTFSPTYKA 569 A*0201 2 1.62 4 18 653 691 669 677 9 FTFSPTYKA 569 A*6802 47 1.62 76 18 653 691 669 677 9 FTFSPTYKA 569 B*5601 36 1.62 58 18 653 691 668 678 11 AFTFSPTYKAF 570 A*2402 14 0.94 13 18 653 691 669 678 10 FTFSPTYKAF 571 A*0101 64 0.94 60 18 653 691 669 678 10 FTFSPTYKAF 571 A*2501 96 0.94 90 18 653 691 669 678 10 FTFSPTYKAF 571 A*2601 92 0.94 87 18 653 691 669 678 10 FTFSPTYKAF 571 B*1501 88 0.94 82 18 653 691 669 678 10 FTFSPTYKAF 571 B*1502 100 0.94 94 18 653 691 669 678 10 FTFSPTYKAF 571 B*1525 83 0.94 78 18 653 691 669 678 10 FTFSPTYKAF 571 B*3501 36 0.94 34 18 653 691 669 678 10 FTFSPTYKAF 571 B*3503 43 0.94 41 18 653 691 669 678 10 FTFSPTYKAF 571 B*4601 98 0.94 92 18 653 691 669 678 10 FTFSPTYKAF 571 B*5802 48 0.94 45 18 653 691 670 678 9 TFSPTYKAF 572 A*2301 83 0.94 78 18 653 691 670 678 9 TFSPTYKAF 572 A*2402 42 0.94 39 18 653 691 669 679 11 FTFSPTYKAFL 573 A*2501 61 0.51 32 18 653 691 669 679 11 FTFSPTYKAFL 573 A*2601 46 0.51 24 18 653 691 669 679 11 FTFSPTYKAFL 573 B*4601 61 0.51 31 18 653 691 672 679 8 SPTYKAFL 574 B*0801 39 0.51 20 18 653 691 672 679 8 SPTYKAFL 574 B*3503 15 0.51 8 18 653 691 672 679 8 SPTYKAFL 574 B*5501 1 0.51 1 18 653 691 673 681 9 PTYKAFLSK 575 A*0301 72 1.52 110 18 653 691 673 681 9 PTYKAFLSK 575 A*1101 61 1.52 92 18 653 691 674 681 8 TYKAFLSK 576 A*3001 77 1.52 117 18 653 691 674 681 8 TYKAFLSK 576 A*3101 18 1.52 27 18 653 691 673 683 11 PTYKAFLSKQY 577 A*0101 47 1.56 73 18 653 691 673 683 11 PTYKAFLSKQY 577 A*2902 8 1.56 12 18 653 691 673 683 11 PTYKAFLSKQY 577 A*3002 27 1.56 42 18 653 691 674 683 10 TYKAFLSKQY 578 A*2902 67 1.56 104 18 653 691 674 683 10 TYKAFLSKQY 578 A*3002 21 1.56 33 18 653 691 676 683 8 KAFLSKQY 579 A*3002 51 1.56 79 18 653 691 676 683 8 KAFLSKQY 579 B*1501 25 1.56 39 18 653 691 676 683 8 KAFLSKQY 579 B*1502 11 1.56 17 18 653 691 676 683 8 KAFLSKQY 579 B*1525 61 1.56 95 18 653 691 676 683 8 KAFLSKQY 579 B*5701 71 1.56 111 18 653 691 676 683 8 KAFLSKQY 579 B*5801 51 1.56 79 18 653 691 676 683 8 KAFLSKQY 579 B*5802 62 1.56 97 18 653 691 676 684 9 KAFLSKQYM 580 B*5701 82 1.51 124 18 653 691 676 684 9 KAFLSKQYM 580 B*5801 46 1.51 69 18 653 691 676 685 10 KAFLSKQYMN 581 A*3001 63 1.51 24 18 653 691 676 686 11 KAFLSKQYMNL 582 A*3001 48 1.83 88 18 653 691 676 686 11 KAFLSKQYMNL 582 A*3201 24 1.83 44 18 653 691 676 686 11 KAFLSKQYMNL 582 B*4801 13 1.83 25 18 653 691 676 686 11 KAFLSKQYMNL 582 B*5701 62 1.83 114 18 653 691 676 686 11 KAFLSKQYMNL 582 B*5801 19 1.83 34 18 653 691 676 686 11 KAFLSKQYMNL 582 B*5802 23 1.83 43 18 653 691 678 686 9 FLSKQYMNL 583 A*0201 33 1.83 61 18 653 691 677 687 11 AFLSKQYMNLY 584 A*2902 84 1.58 133 18 653 691 677 687 11 AFLSKQYMNLY 584 A*3002 55 1.58 87 18 653 691 678 687 10 FLSKQYMNLY 585 A*0101 98 1.58 155 18 653 691 678 687 10 FLSKQYMNLY 585 A*2501 67 1.58 106 18 653 691 678 687 10 FLSKQYMNLY 585 A*3002 34 1.58 53 18 653 691 678 687 10 FLSKQYMNLY 585 B*1501 23 1.58 37 18 653 691 678 687 10 FLSKQYMNLY 585 B*1502 35 1.58 56 18 653 691 678 687 10 FLSKQYMNLY 585 B*4601 18 1.58 28 18 653 691 679 687 9 LSKQYMNLY 586 A*0101 96 1.58 152 18 653 691 679 687 9 LSKQYMNLY 586 A*3002 69 1.58 109 18 653 691 679 687 9 LSKQYMNLY 586 B*1501 27 1.58 42 18 653 691 680 687 8 SKQYMNLY 587 B*3501 21 1.59 34 18 653 691 679 689 11 LSKQYMNLYPV 588 B*0801 37 0.93 35 18 653 691 681 689 9 KQYMNLYPV 589 A*0201 89 0.93 83 18 653 691 681 689 9 KQYMNLYPV 589 A*0206 96 0.93 89 18 653 691 681 689 9 KQYMNLYPV 589 A*3201 44 0.93 41 18 653 691 681 689 9 KQYMNLYPV 589 B*1301 72 0.93 67 18 653 691 681 689 9 KQYMNLYPV 589 B*1302 38 0.93 35 18 653 691 681 689 9 KQYMNLYPV 589 B*1525 29 0.93 27 18 653 691 681 689 9 KQYMNLYPV 589 B*2702 48 0.93 45 18 653 691 681 689 9 KQYMNLYPV 589 B*4801 88 0.93 82 18 653 691 681 689 9 KQYMNLYPV 589 B*5001 48 0.93 45 18 653 691 681 689 9 KQYMNLYPV 589 B*5201 73 0.93 67 18 653 691 682 689 8 QYMNLYPV 590 A*2301 59 0.93 54 18 653 691 682 689 8 QYMNLYPV 590 A*2402 61 0.93 57 18 653 691 681 690 10 KQYMNLYPVA 591 B*1302 3 1.25 4 18 653 691 681 690 10 KQYMNLYPVA 591 B*4801 42 1.25 53 18 653 691 681 690 10 KQYMNLYPVA 591 B*5001 16 1.25 20 18 653 691 681 691 11 KQYMNLYPVAR 592 A*0301 49 1.78 88 18 653 691 681 691 11 KQYMNLYPVAR 592 A*3101 100 1.78 178 18 653 691 681 691 11 KQYMNLYPVAR 592 A*3201 23 1.78 40 18 653 691 681 691 11 KQYMNLYPVAR 592 A*7401 100 1.78 178 18 653 691 682 691 10 QYMNLYPVAR 593 A*3101 84 1.78 149 18 653 691 682 691 10 QYMNLYPVAR 593 A*3303 90 1.78 160 18 653 691 683 691 9 YMNLYPVAR 594 A*3101 78 1.78 140 18 653 691 683 691 9 YMNLYPVAR 594 A*3303 89 1.78 158 18 653 691 683 691 9 YMNLYPVAR 594 A*7401 94 1.78 167 18 653 691 684 691 8 MNLYPVAR 595 A*3101 16 1.78 29 18 653 691 684 691 8 MNLYPVAR 595 A*3303 75 1.78 133 18 653 691 Cumulative Class I-BCI score: 12576 657 665 9 MPLYACIQA 556 B*3501 44 1.41 62 19 657 691 657 665 9 MPLYACIQA 556 B*3503 49 1.41 68 19 657 691 657 665 9 MPLYACIQA 556 B*5101 80 1.41 112 19 657 691 657 665 9 MPLYACIQA 556 B*5501 93 1.41 131 19 657 691 657 665 9 MPLYACIQA 556 B*5601 99 1.41 139 19 657 691 657 666 10 MPLYACIQAK 557 B*3501 43 1.01 43 19 657 691 657 666 10 MPLYACIQAK 557 B*5601 3 1.01 3 19 657 691 658 666 9 PLYACIQAK 558 A*0301 74 1.01 75 19 657 691 659 669 11 LYACIQAKQAF 559 A*2301 86 1.07 92 19 657 691 659 669 11 LYACIQAKQAF 559 A*2402 88 1.07 94 19 657 691 660 669 10 YACIQAKQAF 560 B*1502 26 1.07 28 19 657 691 663 671 9 IQAKQAFTF 561 A*2402 84 1.58 133 19 657 691 663 671 9 IQAKQAFTF 561 B*1301 61 1.58 96 19 657 691 663 671 9 IQAKQAFTF 561 B*1501 63 1.58 99 19 657 691 663 671 9 IQAKQAFTF 561 B*1525 71 1.58 112 19 657 691 664 671 8 QAKQAFTF 562 B*1501 8 1.58 12 19 657 691 664 671 8 QAKQAFTF 562 B*1502 37 1.58 59 19 657 691 664 671 8 QAKQAFTF 562 B*1525 14 1.58 21 19 657 691 664 671 8 QAKQAFTF 562 B*5802 3 1.58 5 19 657 691 666 675 10 KQAFTFSPTY 563 A*2902 27 1.81 49 19 657 691 666 675 10 KQAFTFSPTY 563 A*3002 30 1.81 53 19 657 691 666 675 10 KQAFTFSPTY 563 B*1501 89 1.81 161 19 657 691 666 675 10 KQAFTFSPTY 563 B*1502 63 1.81 114 19 657 691 666 675 10 KQAFTFSPTY 563 B*1525 85 1.81 153 19 657 691 666 675 10 KQAFTFSPTY 563 B*5001 32 1.81 58 19 657 691 667 675 9 QAFTFSPTY 564 A*2902 46 1.81 83 19 657 691 667 675 9 QAFTFSPTY 564 A*3002 58 1.81 104 19 657 691 667 675 9 QAFTFSPTY 564 B*1525 66 1.81 119 19 657 691 667 675 9 QAFTFSPTY 564 B*3501 73 1.81 133 19 657 691 667 675 9 QAFTFSPTY 564 B*5701 12 1.81 22 19 657 691 668 675 8 AFTFSPTY 565 A*2902 60 1.81 109 19 657 691 668 675 8 AFTFSPTY 565 A*3002 56 1.81 102 19 657 691 666 676 11 KQAFTFSPTYK 566 A*0301 100 1.78 178 19 657 691 666 676 11 KQAFTFSPTYK 566 A*1101 83 1.78 147 19 657 691 666 676 11 KQAFTFSPTYK 566 A*3001 49 1.78 87 19 657 691 666 676 11 KQAFTFSPTYK 566 A*7401 60 1.78 106 19 657 691 667 676 10 QAFTFSPTYK 567 A*0301 64 1.78 114 19 657 691 667 676 10 QAFTFSPTYK 567 A*1101 78 1.78 139 19 657 691 667 676 10 QAFTFSPTYK 567 A*6801 91 1.78 162 19 657 691 667 676 10 QAFTFSPTYK 567 A*7401 59 1.78 104 19 657 691 669 676 8 FTFSPTYK 568 A*0301 98 1.78 175 19 657 691 669 676 8 FTFSPTYK 568 A*1101 96 1.78 170 19 657 691 669 676 8 FTFSPTYK 568 A*3101 25 1.78 45 19 657 691 669 676 8 FTFSPTYK 568 A*3303 69 1.78 123 19 657 691 669 676 8 FTFSPTYK 568 A*7401 99 1.78 176 19 657 691 669 677 9 FTFSPTYKA 569 A*0201 2 1.62 4 19 657 691 669 677 9 FTFSPTYKA 569 A*6802 47 1.62 76 19 657 691 669 677 9 FTFSPTYKA 569 B*5601 36 1.62 58 19 657 691 668 678 11 AFTFSPTYKAF 570 A*2402 14 0.94 13 19 657 691 669 678 10 FTFSPTYKAF 571 A*0101 64 0.94 60 19 657 691 669 678 10 FTFSPTYKAF 571 A*2501 96 0.94 90 19 657 691 669 678 10 FTFSPTYKAF 571 A*2601 92 0.94 87 19 657 691 669 678 10 FTFSPTYKAF 571 B*1501 88 0.94 82 19 657 691 669 678 10 FTFSPTYKAF 571 B*1502 100 0.94 94 19 657 691 669 678 10 FTFSPTYKAF 571 B*1525 83 0.94 78 19 657 691 669 678 10 FTFSPTYKAF 571 B*3501 36 0.94 34 19 657 691 669 678 10 FTFSPTYKAF 571 B*3503 43 0.94 41 19 657 691 669 678 10 FTFSPTYKAF 571 B*4601 98 0.94 92 19 657 691 669 678 10 FTFSPTYKAF 571 B*5802 48 0.94 45 19 657 691 670 678 9 TFSPTYKAF 572 A*2301 83 0.94 78 19 657 691 670 678 9 TFSPTYKAF 572 A*2402 42 0.94 39 19 657 691 669 679 11 FTFSPTYKAFL 573 A*2501 61 0.51 32 19 657 691 669 679 11 FTFSPTYKAFL 573 A*2601 46 0.51 24 19 657 691 669 679 11 FTFSPTYKAFL 573 B*4601 61 0.51 31 19 657 691 672 679 8 SPTYKAFL 574 B*0801 39 0.51 20 19 657 691 672 679 8 SPTYKAFL 574 B*3503 15 0.51 8 19 657 691 672 679 8 SPTYKAFL 574 B*5501 1 0.51 1 19 657 691 673 681 9 PTYKAFLSK 575 A*0301 72 1.52 110 19 657 691 673 681 9 PTYKAFLSK 575 A*1101 61 1.52 92 19 657 691 674 681 8 TYKAFLSK 576 A*3001 77 1.52 117 19 657 691 674 681 8 TYKAFLSK 576 A*3101 18 1.52 27 19 657 691 673 683 11 PTYKAFLSKQY 577 A*0101 47 1.56 73 19 657 691 673 683 11 PTYKAFLSKQY 577 A*2902 8 1.56 12 19 657 691 673 683 11 PTYKAFLSKQY 577 A*3002 27 1.56 42 19 657 691 674 683 10 TYKAFLSKQY 578 A*2902 67 1.56 104 19 657 691 674 683 10 TYKAFLSKQY 578 A*3002 21 1.56 33 19 657 691 676 683 8 KAFLSKQY 579 A*3002 51 1.56 79 19 657 691 676 683 8 KAFLSKQY 579 B*1501 25 1.56 39 19 657 691 676 683 8 KAFLSKQY 579 B*1502 11 1.56 17 19 657 691 676 683 8 KAFLSKQY 579 B*1525 61 1.56 95 19 657 691 676 683 8 KAFLSKQY 579 B*5701 71 1.56 111 19 657 691 676 683 8 KAFLSKQY 579 B*5801 51 1.56 79 19 657 691 676 683 8 KAFLSKQY 579 B*5802 62 1.56 97 19 657 691 676 684 9 KAFLSKQYM 580 B*5701 82 1.51 124 19 657 691 676 684 9 KAFLSKQYM 580 B*5801 46 1.51 69 19 657 691 676 685 10 KAFLSKQYMN 581 A*3001 63 1.51 24 19 657 691 676 686 11 KAFLSKQYMNL 582 A*3001 48 1.83 88 19 657 691 676 686 11 KAFLSKQYMNL 582 A*3201 24 1.83 44 19 657 691 676 686 11 KAFLSKQYMNL 582 B*4801 13 1.83 25 19 657 691 676 686 11 KAFLSKQYMNL 582 B*5701 62 1.83 114 19 657 691 676 686 11 KAFLSKQYMNL 582 B*5801 19 1.83 34 19 657 691 676 686 11 KAFLSKQYMNL 582 B*5802 23 1.83 43 19 657 691 678 686 9 FLSKQYMNL 583 A*0201 33 1.83 61 19 657 691 677 687 11 AFLSKQYMNLY 584 A*2902 84 1.58 133 19 657 691 677 687 11 AFLSKQYMNLY 584 A*3002 55 1.58 87 19 657 691 678 687 10 FLSKQYMNLY 585 A*0101 98 1.58 155 19 657 691 678 687 10 FLSKQYMNLY 585 A*2501 67 1.58 106 19 657 691 678 687 10 FLSKQYMNLY 585 A*3002 34 1.58 53 19 657 691 678 687 10 FLSKQYMNLY 585 B*1501 23 1.58 37 19 657 691 678 687 10 FLSKQYMNLY 585 B*1502 35 1.58 56 19 657 691 678 687 10 FLSKQYMNLY 585 B*4601 18 1.58 28 19 657 691 679 687 9 LSKQYMNLY 586 A*0101 96 1.58 152 19 657 691 679 687 9 LSKQYMNLY 586 A*3002 69 1.58 109 19 657 691 679 687 9 LSKQYMNLY 586 B*1501 27 1.58 42 19 657 691 680 687 8 SKQYMNLY 587 B*3501 21 1.58 34 19 657 691 679 689 11 LSKQYMNLYPV 588 B*0801 37 0.93 35 19 657 691 681 689 9 KQYMNLYPV 589 A*0201 89 0.93 83 19 657 691 681 689 9 KQYMNLYPV 589 A*0206 96 0.93 89 19 657 691 681 689 9 KQYMNLYPV 589 A*3201 44 0.93 41 19 657 691 681 689 9 KQYMNLYPV 589 B*1301 72 0.93 67 19 657 691 681 689 9 KQYMNLYPV 589 B*1302 38 0.93 35 19 657 691 681 689 9 KQYMNLYPV 589 B*1525 29 0.93 27 19 657 691 681 689 9 KQYMNLYPV 589 B*2702 48 0.93 45 19 657 691 681 689 9 KQYMNLYPV 589 B*4801 88 0.93 82 19 657 691 681 689 9 KQYMNLYPV 589 B*5001 48 0.93 45 19 657 691 681 689 9 KQYMNLYPV 589 B*5201 73 0.93 67 19 657 691 682 689 8 QYMNLYPV 590 A*2301 59 0.93 54 19 657 691 682 689 8 QYMNLYPV 590 A*2402 61 0.93 57 19 657 691 681 690 10 KQYMNLYPVA 591 B*1302 3 1.25 4 19 657 691 681 690 10 KQYMNLYPVA 591 B*4801 42 1.25 53 19 657 691 681 690 10 KQYMNLYPVA 591 B*5001 16 1.25 20 19 657 691 681 691 11 KQYMNLYPVAR 592 A*0301 49 1.78 88 19 657 691 681 691 11 KQYMNLYPVAR 592 A*3101 100 1.78 178 19 657 691 681 691 11 KQYMNLYPVAR 592 A*3201 23 1.78 40 19 657 691 681 691 11 KQYMNLYPVAR 592 A*7401 100 1.78 178 19 657 691 682 691 10 QYMNLYPVAR 593 A*3101 84 1.78 149 19 657 691 682 691 10 QYMNLYPVAR 593 A*3303 90 1.78 160 19 657 691 683 691 9 YMNLYPVAR 594 A*3101 78 1.78 140 19 657 691 683 691 9 YMNLYPVAR 594 A*3303 89 1.78 158 19 657 691 683 691 9 YMNLYPVAR 594 A*7401 94 1.78 167 19 657 691 684 691 8 MNLYPVAR 595 A*3101 16 1.78 29 19 657 691 684 691 8 MNLYPVAR 595 A*3303 75 1.78 133 19 657 691 Cumulative Class I-BCI score: 10420 716 723 8 RMRGTFVA 596 A*3001 92 1.41 130 20 715 746 716 724 9 RMRGTFVAP 597 A*3001 7 0.12 1 20 715 746 717 724 8 MRGTFVAP 598 A*0206 94 0.12 11 20 715 746 715 725 11 QRMRGTFVAPL 599 B*1402 89 0.99 88 20 715 746 715 725 11 QRMRGTFVAPL 599 B*2702 83 0.99 82 20 715 746 715 725 11 QRMRGTFVAPL 599 B*3801 57 0.99 57 20 715 746 715 725 11 QRMRGTFVAPL 599 B*3901 99 0.99 98 20 715 746 715 725 11 QRMRGTFVAPL 599 B*4801 29 0.99 29 20 715 746 716 725 10 RMRGTFVAPL 600 B*0801 76 0.99 76 20 715 746 716 725 10 RMRGTFVAPL 600 B*1402 65 0.99 64 20 715 746 716 725 10 RMRGTFVAPL 600 B*1501 67 0.99 67 20 715 746 716 725 10 RMRGTFVAPL 600 B*1525 47 0.99 47 20 715 746 716 725 10 RMRGTFVAPL 600 B*4801 90 0.99 90 20 715 746 717 725 9 MRGTFVAPL 601 B*1402 88 0.99 87 20 715 746 717 725 9 MRGTFVAPL 601 B*2702 71 0.99 70 20 715 746 717 725 9 MRGTFVAPL 601 B*3901 81 0.99 80 20 715 746 716 726 11 RMRGTFVAPLP 602 A*3001 37 0.08 3 20 715 746 718 726 9 RGTFVAPLP 603 B*5802 45 0.08 4 20 715 746 717 727 11 MRGTFVAPLPI 604 B*1402 70 0.98 68 20 715 746 717 727 11 MRGTFVAPLPI 604 B*2702 82 0.98 80 20 715 746 717 727 11 MRGTFVAPLPI 604 B*3801 37 0.98 36 20 715 746 717 727 11 MRGTFVAPLPI 604 B*3901 49 0.98 48 20 715 746 717 727 11 MRGTFVAPLPI 604 B*5201 18 0.98 17 20 715 746 719 727 9 GTFVAPLPI 605 A*3201 70 0.98 68 20 715 746 719 727 9 GTFVAPLPI 605 B*5201 59 0.98 58 20 715 746 720 727 8 TFVAPLPI 606 A*2301 19 0.98 19 20 715 746 720 727 8 TFVAPLPI 606 A*2402 12 0.98 12 20 715 746 719 728 10 GTFVAPLPIH 607 A*3001 97 0.37 36 20 715 746 721 730 10 FVAPLPIHTA 608 A*0206 58 1.82 106 20 715 746 721 730 10 FVAPLPIHTA 608 B*5601 51 1.82 94 20 715 746 723 730 8 APLPIHTA 609 B*5501 67 1.82 123 20 715 746 723 730 8 APLPIHTA 609 B*5601 76 1.82 138 20 715 746 723 732 10 APLPIHTAEL 610 B*0702 67 1.48 99 20 715 746 723 732 10 APLPIHTAEL 610 B*1402 69 1.48 102 20 715 746 723 732 10 APLPIHTAEL 610 B*3503 66 1.48 98 20 715 746 723 732 10 APLPIHTAEL 610 B*5501 53 1.48 79 20 715 746 723 732 10 APLPIHTAEL 610 B*5601 44 1.48 65 20 715 746 725 732 8 LPIHTAEL 611 B*1402 76 1.48 112 20 715 746 725 732 8 LPIHTAEL 611 B*3503 89 1.48 132 20 715 746 725 732 8 LPIHTAEL 611 B*3901 48 1.48 71 20 715 746 725 732 8 LPIHTAEL 611 B*5101 88 1.48 131 20 715 746 725 732 8 LPIHTAEL 611 B*5301 77 1.48 114 20 715 746 725 732 8 LPIHTAEL 611 B*5501 74 1.48 110 20 715 746 725 732 8 LPIHTAEL 611 B*5601 71 1.48 104 20 715 746 723 733 11 APLPIHTAELL 612 B*0702 33 1.70 57 20 715 746 723 733 11 APLPIHTAELL 612 B*1402 39 1.70 67 20 715 746 725 733 9 LPIHTAELL 613 B*0702 1 1.70 2 20 715 746 725 733 9 LPIHTAELL 613 B*1402 38 1.70 65 20 715 746 725 733 9 LPIHTAELL 613 B*3503 57 1.70 97 20 715 746 725 733 9 LPIHTAELL 613 B*5101 78 1.70 133 20 715 746 725 733 9 LPIHTAELL 613 B*5301 61 1.70 103 20 715 746 725 733 9 LPIHTAELL 613 B*5501 10 1.70 18 20 715 746 725 733 9 LPIHTAELL 613 B*5601 26 1.70 44 20 715 746 725 734 10 LPIHTAELLA 614 B*3503 42 1.12 47 20 715 746 725 734 10 LPIHTAELLA 614 B*5501 81 1.12 91 20 715 746 725 734 10 LPIHTAELLA 614 B*5601 92 1.12 103 20 715 746 725 735 11 LPIHTAELLAA 615 B*0702 45 1.10 49 20 715 746 725 735 11 LPIHTAELLAA 615 B*3501 76 1.10 84 20 715 746 725 735 11 LPIHTAELLAA 615 B*3503 65 1.10 71 20 715 746 725 735 11 LPIHTAELLAA 615 B*5101 45 1.10 49 20 715 746 725 735 11 LPIHTAELLAA 615 B*5501 92 1.10 101 20 715 746 725 735 11 LPIHTAELLAA 615 B*5601 97 1.10 107 20 715 746 728 735 8 HTAELLAA 616 A*2501 31 1.10 34 20 715 746 728 735 8 HTAELLAA 616 A*2601 72 1.10 79 20 715 746 728 735 8 HTAELLAA 616 B*5501 9 1.10 10 20 715 746 728 735 8 HTAELLAA 616 B*5601 32 1.10 35 20 715 746 728 736 9 HTAELLAAC 617 A*2501 86 0.20 18 20 715 746 728 736 9 HTAELLAAC 617 A*2601 54 0.20 11 20 715 746 728 737 10 HTAELLAACF 618 A*0101 32 1.63 52 20 715 746 728 737 10 HTAELLAACF 618 A*2501 94 1.63 153 20 715 746 728 737 10 HTAELLAACF 618 A*2601 85 1.63 138 20 715 746 728 737 10 HTAELLAACF 618 B*1502 43 1.63 69 20 715 746 728 737 10 HTAELLAACF 618 B*4601 72 1.63 117 20 715 746 728 737 10 HTAELLAACF 618 B*5802 42 1.63 68 20 715 746 730 737 8 AELLAACF 619 B*1301 65 1.63 105 20 715 746 730 737 8 AELLAACF 619 B*1801 76 1.63 124 20 715 746 730 737 8 AELLAACF 619 B*4001 70 1.63 113 20 715 746 730 737 8 AELLAACF 619 B*4002 65 1.63 106 20 715 746 730 737 8 AELLAACF 619 B*4403 96 1.63 156 20 715 746 730 737 8 AELLAACF 619 B*4901 52 1.63 85 20 715 746 730 737 8 AELLAACF 619 B*5001 40 1.63 65 20 715 746 728 738 11 HTAELLAACFA 620 A*2601 36 0.81 29 20 715 746 730 738 9 AELLAACFA 621 B*1301 59 0.81 48 20 715 746 730 738 9 AELLAACFA 621 B*1302 10 0.81 8 20 715 746 730 738 9 AELLAACFA 621 B*3701 29 0.81 23 20 715 746 730 738 9 AELLAACFA 621 B*4002 85 0.81 69 20 715 746 730 738 9 AELLAACFA 621 B*4402 73 0.81 59 20 715 746 730 738 9 AELLAACFA 621 B*4403 68 0.81 55 20 715 746 730 738 9 AELLAACFA 621 B*4901 65 0.81 53 20 715 746 730 738 9 AELLAACFA 621 B*5001 72 0.81 59 20 715 746 729 739 11 TAELLAACFAR 622 A*6801 54 1.51 82 20 715 746 730 739 10 AELLAACFAR 623 B*4002 45 1.51 68 20 715 746 731 739 9 ELLAACFAR 624 A*3303 80 1.51 121 20 715 746 731 739 9 ELLAACFAR 624 A*6801 71 1.51 107 20 715 746 731 739 9 ELLAACFAR 624 A*7401 18 1.51 28 20 715 746 732 739 8 LLAACFAR 625 A*3101 24 1.51 36 20 715 746 732 739 8 LLAACFAR 625 A*3303 66 1.51 100 20 715 746 732 739 8 LLAACFAR 625 A*6801 57 1.51 87 20 715 746 732 739 8 LLAACFAR 625 A*7401 93 1.51 140 20 715 746 730 740 11 AELLAACFARS 626 B*4402 12 0.24 3 20 715 746 730 740 11 AELLAACFARS 626 B*4403 4 0.24 1 20 715 746 733 740 8 LAACFARS 627 A*0206 13 0.24 3 20 715 746 731 741 11 ELLAACFARSR 628 A*3303 37 1.17 43 20 715 746 732 741 10 LLAACFARSR 629 A*3101 58 1.17 68 20 715 746 732 741 10 LLAACFARSR 629 A*3303 6 1.17 7 20 715 746 732 741 10 LLAACFARSR 629 A*7401 66 1.17 77 20 715 746 733 741 9 LAACFARSR 630 A*3303 28 1.17 33 20 715 746 733 741 9 LAACFARSR 630 A*6801 56 1.17 66 20 715 746 734 741 8 AACFARSR 631 A*3101 15 1.17 18 20 715 746 737 744 8 FARSRSGA 632 B*0801 85 0.75 63 20 715 746 737 744 8 FARSRSGA 632 B*5501 59 0.75 44 20 715 746 737 744 8 FARSRSGA 632 B*5601 1 0.75 1 20 715 746 737 745 9 FARSRSGAK 633 A*3001 39 0.48 19 20 715 746 737 745 9 FARSRSGAK 633 B*5501 16 0.48 8 20 715 746 737 746 10 FARSRSGAKL 634 B*1402 25 1.60 41 20 715 746 737 746 10 FARSRSGAKL 634 B*4601 3 1.60 5 20 715 746 737 746 10 FARSRSGAKL 634 B*5501 15 1.60 24 20 715 746 738 746 9 ARSRSGAKL 635 B*2702 12 1.60 19 20 715 746 739 746 8 RSRSGAKL 636 A*3001 76 1.60 122 20 715 746 Cumulative BCI Class Iscore: 7869 754 762 9 VLSRKYTSF 638 B*0801 68 1.77 120 21 754 791 754 762 9 VLSRKYTSF 638 B*1501 17 1.77 30 21 754 791 755 762 8 LSRKYTSF 639 B*0801 61 1.77 108 21 754 791 755 762 8 LSRKYTSF 639 B*1501 98 1.77 174 21 754 791 755 762 8 LSRKYTSF 639 B*1502 85 1.77 150 21 754 791 755 762 8 LSRKYTSF 639 B*1525 81 1.77 144 21 754 791 755 762 8 LSRKYTSF 639 B*4601 59 1.77 104 21 754 791 755 762 8 LSRKYTSF 639 B*5701 61 1.77 107 21 754 791 755 762 8 LSRKYTSF 639 B*5802 46 1.77 82 21 754 791 754 764 11 VLSRKYTSFPW 640 A*3201 17 0.99 16 21 754 791 754 764 11 VLSRKYTSFPW 640 B*5701 55 0.99 54 21 754 791 754 764 11 VLSRKYTSFPW 640 B*5801 56 0.99 55 21 754 791 754 764 11 VLSRKYTSFPW 640 B*5802 22 0.99 21 21 754 791 755 764 10 LSRKYTSFPW 641 B*1525 10 0.99 10 21 754 791 755 764 10 LSRKYTSFPW 641 B*5802 96 0.99 94 21 754 791 756 764 9 SRKYTSFPW 642 B*2702 81 0.99 80 21 754 791 757 764 8 RKYTSFPW 643 B*1301 52 0.99 51 21 754 791 757 764 8 RKYTSFPW 643 B*2702 94 0.99 93 21 754 791 757 764 8 RKYTSFPW 643 B*4402 4 0.99 4 21 754 791 757 764 8 RKYTSFPW 643 B*4403 12 0.99 12 21 754 791 757 764 8 RKYTSFPW 643 B*5701 3 0.99 3 21 754 791 757 764 8 RKYTSFPW 643 B*5802 12 0.99 11 21 754 791 755 765 11 LSRKYTSFPWL 644 A*3001 36 1.24 45 21 754 791 755 765 11 LSRKYTSFPWL 644 B*0801 36 1.24 44 21 754 791 756 765 10 SRKYTSFPWL 645 A*3001 21 1.24 26 21 754 791 756 765 10 SRKYTSFPWL 645 B*1402 24 1.24 30 21 754 791 756 765 10 SRKYTSFPWL 645 B*2702 46 1.24 57 21 754 791 756 765 10 SRKYTSFPWL 645 B*2705 10 1.24 13 21 754 791 757 765 9 RKYTSFPWL 646 B*1402 8 1.24 10 21 754 791 757 765 9 RKYTSFPWL 646 B*2702 4 1.24 4 21 754 791 757 765 9 RKYTSFPWL 646 B*4801 87 1.24 108 21 754 791 758 765 8 KYTSFPWL 647 A*2301 81 1.24 101 21 754 791 758 765 8 KYTSFPWL 647 A*2402 77 1.24 96 21 754 791 756 766 11 SRKYTSFPWLL 648 B*1402 64 1.92 122 21 754 791 756 766 11 SRKYTSFPWLL 648 B*2702 80 1.92 152 21 754 791 756 766 11 SRKYTSFPWLL 648 B*3901 26 1.92 50 21 754 791 757 766 10 RKYTSFPWLL 649 B*1302 8 1.92 16 21 754 791 757 766 10 RKYTSFPWLL 649 B*1402 63 1.92 120 21 754 791 757 766 10 RKYTSFPWLL 649 B*2702 70 1.92 134 21 754 791 757 766 10 RKYTSFPWLL 649 B*3901 17 1.92 32 21 754 791 757 766 10 RKYTSFPWLL 649 B*4801 75 1.92 144 21 754 791 758 766 9 KYTSFPWLL 650 A*2301 97 1.92 185 21 754 791 758 766 9 KYTSFPWLL 600 A*2402 96 1.92 185 21 754 791 759 766 8 YTSFPWLL 651 A*0101 57 1.92 108 21 754 791 759 766 8 YTSFPWLL 651 A*2601 18 1.92 34 21 754 791 759 766 8 YTSFPWLL 651 B*5801 5 1.92 10 21 754 791 757 767 11 RKYTSFPWLLG 652 B*2705 48 0.64 31 21 754 791 758 767 10 KYTSFPWLLG 653 A*3201 11 0.64 7 21 754 791 759 767 9 YTSFPWLLG 654 A*0101 9 0.64 6 21 754 791 762 769 8 FPWLLGCT 655 B*3501 65 0.19 13 21 754 791 762 769 8 FPWLLGCT 655 B*3503 8 0.19 2 21 754 791 762 769 8 FPWLLGCT 655 B*5101 35 0.19 7 21 754 791 762 769 8 FPWLLGCT 655 B*5501 66 0.19 13 21 754 791 762 769 8 FPWLLGCT 655 B*5601 85 0.19 16 21 754 791 762 770 9 FPWLLGCTA 656 B*1402 14 1.76 25 21 754 791 762 770 9 FPWLLGCTA 656 B*3501 39 1.76 68 21 754 791 762 770 9 FPWLLGCTA 656 B*3503 88 1.76 155 21 754 791 762 770 9 FPWLLGCTA 656 B*5101 33 1.76 59 21 754 791 762 771 10 FPWLLGCTAN 657 B*0702 7 0.39 3 21 754 791 762 771 10 FPWLLGCTAN 657 B*3501 79 0.39 31 21 754 791 762 771 10 FPWLLGCTAN 657 B*3503 24 0.39 9 21 754 791 762 771 10 FPWLLGCTAN 657 B*5101 57 0.39 22 21 754 791 762 771 10 FPWLLGCTAN 657 B*5301 52 0.39 20 21 754 791 762 771 10 FPWLLGCTAN 657 B*5501 52 0.39 20 21 754 791 762 771 10 FPWLLGCTAN 657 B*5601 69 0.39 27 21 754 791 762 772 11 FPWLLGCTANW 658 B*1402 55 1.72 94 21 754 791 762 772 11 FPWLLGCTANW 658 B*1801 48 1.72 82 21 754 791 762 772 11 FPWLLGCTANW 658 B*3501 93 1.72 161 21 754 791 762 772 11 FPWLLGCTANW 658 B*3503 81 1.72 140 21 754 791 762 772 11 FPWLLGCTANW 658 B*3801 63 1.72 109 21 754 791 762 772 11 FPWLLGCTANW 658 B*5101 87 1.72 149 21 754 791 762 772 11 FPWLLGCTANW 658 B*5501 8 1.72 14 21 754 791 762 772 11 FPWLLGCTANW 658 B*5601 50 1.72 86 21 754 791 763 772 10 PWLLGCTANW 659 A*2301 67 1.72 116 21 754 791 763 772 10 PWLLGCTANW 659 A*2402 32 1.72 54 21 754 791 764 772 9 WLLGCTANW 660 B*5701 26 1.72 44 21 754 791 764 773 10 WLLGcTANWI 661 A*0201 91 0.22 20 21 754 791 765 773 9 LLGCTANWI 662 A*0201 71 0.22 15 21 754 791 764 774 11 WLLGCTANWIL 663 B*3801 18 1.41 26 21 754 791 764 774 11 WLLGCTANWIL 663 B*3901 74 1.41 104 21 754 791 764 774 11 WLLGCTANWIL 663 B*4801 40 1.41 57 21 754 791 765 774 10 LLGCtANWIL 664 A*0201 64 1.41 90 21 754 791 765 775 11 LLGCTANWILR 665 A*7401 30 1.01 31 21 754 791 766 775 10 LGCTANWILR 666 A*3201 33 1.01 34 21 754 791 768 775 8 CTANWILR 667 A*1101 72 1.01 72 21 754 791 768 775 8 CTANWILR 667 A*3101 53 1.01 54 21 754 791 768 775 8 CTANWILR 667 A*3303 79 1.01 80 21 754 791 768 775 8 CTANWILR 667 A*6801 94 1.01 95 21 754 791 768 775 8 CTANWILR 667 A*7401 74 1.01 75 21 754 791 769 779 11 TANWILRGTSF 668 B*1502 33 1.20 40 21 754 791 769 779 11 TANWILRGTSF 668 B*3501 11 1.20 13 21 754 791 769 779 11 TANWILRGTSF 668 B*4601 25 1.20 29 21 754 791 769 779 11 TANWILRGTSF 668 B*5802 20 1.20 24 21 754 791 770 779 10 ANWILRGTSF 669 B*4402 8 1.20 9 21 754 791 771 779 9 NWILRGTSF 670 A*2301 2 1.20 2 21 754 791 771 779 9 NWILRGTSF 670 A*2402 30 1.20 36 21 754 791 772 779 8 WILRGTSF 671 B*0801 7 1.20 8 21 754 791 772 779 8 WILRGTSF 671 B*1501 52 1.20 62 21 754 791 772 779 8 WILRGTSF 671 B*1502 81 1.20 97 21 754 791 772 779 8 WILRGTSF 671 B*1525 63 1.20 75 21 754 791 772 779 8 WILRGTSF 671 B*4601 39 1.20 47 21 754 791 772 780 9 WILRGTSFV 672 A*0201 100 1.19 119 21 754 791 772 780 9 WILRGTSFV 672 A*0206 69 1.19 82 21 754 791 771 781 11 NWILRGTSFVY 673 A*2902 51 1.69 86 21 754 791 771 781 11 NWILRGTSFVY 673 B*1801 24 1.69 40 21 754 791 772 781 10 WILRGTSFVY 674 B*1502 59 1.69 100 21 754 791 772 781 10 WILRGTSFVY 674 B*1525 8 1.69 14 21 754 791 772 781 10 WILRGTSFVY 674 B*4601 2 1.69 3 21 754 791 773 781 9 ILRGTSFVY 675 A*0301 23 1.69 39 21 754 791 773 781 9 ILRGTSFVY 675 A*2902 63 1.69 108 21 754 791 773 781 9 ILRGTSFVY 675 A*3002 72 1.69 122 21 754 791 773 781 9 ILRGTSFVY 675 B*1501 83 1.69 140 21 754 791 773 781 9 ILRGTSFVY 675 B*1525 69 1.69 118 21 754 791 774 781 8 LRGTSFVY 676 B*2702 23 1.69 39 21 754 791 774 781 8 LRGTSFVY 676 B*2705 37 1.69 63 21 754 791 773 782 10 ILRGTSFVYV 677 A*0201 71 1.67 119 21 754 791 776 785 10 GTSFVYVPSA 678 A*3001 73 1.35 98 21 754 791 776 785 10 GTSFVYVPSA 678 B*5701 45 1.35 61 21 754 791 778 786 9 SFVYVPSAL 679 B*1402 7 1.57 11 21 754 791 779 786 8 FVYVPSAL 680 A*2501 27 1.57 42 21 754 791 779 786 8 FVYVPSAL 600 B*0801 5 1.57 8 21 754 791 779 786 8 FVYVPSAL 680 B*1402 75 1.57 118 21 754 791 779 786 8 FVYVPSAL 680 B*1502 54 1.57 85 21 754 791 779 786 8 FVYVPSAL 680 B*3503 41 1.57 64 21 754 791 779 786 8 FVYVPSAL 680 B*3801 41 1.57 64 21 754 791 779 786 8 FVYVPSAL 680 B*3901 73 1.57 114 21 754 791 779 786 8 FVYVPSAL 680 B*4601 77 1.57 121 21 754 791 779 786 8 FVYVPSAL 680 B*5501 45 1.57 71 21 754 791 779 786 8 FVYVPSAL 680 B*5601 24 1.57 38 21 754 791 781 788 8 YVPSALNP 681 A*0206 73 0.38 27 21 754 791 779 789 11 FVYVPSALNPA 682 A*6802 15 0.68 10 21 754 791 779 789 11 FVYVPSALNPA 682 B*4601 67 0.68 46 21 754 791 779 789 11 FVYVPSALNPA 682 B*5501 65 0.68 44 21 754 791 779 789 11 FVYVPSALNPA 682 B*5601 74 0.68 51 21 754 791 781 789 9 YVPSALNPA 683 A*0206 42 0.68 28 21 754 791 782 789 8 VPSALNPA 684 B*0702 22 0.68 15 21 754 791 782 789 8 VPSALNPA 684 B*3503 1 0.68 1 21 754 791 782 789 8 VPSALNPA 684 B*5101 5 0.68 3 21 754 791 782 789 8 VPSALNPA 684 B*5501 80 0.68 55 21 754 791 782 789 8 VPSALNPA 684 B*5601 91 0.68 62 21 754 791 781 790 10 YVPSALNPAD 685 A*3001 14 0.18 3 21 754 791 Cumulative Class I-BCI score: 8555 757 765 9 RKYTSFPWL 646 B*1402 8 1.24 10 22 757 792 757 765 9 RKYTSFPWL 646 B*2702 4 1.24 4 22 757 792 757 765 9 RKYTSFPWL 646 B*4801 87 1.24 108 22 757 792 758 765 8 KYTSFPWL 647 A*2301 81 1.24 101 22 757 792 758 765 8 KYTSFPWL 647 A*2402 77 1.24 96 22 757 792 756 766 11 SRKYTSFPWLL 648 B*1402 64 1.92 122 22 757 792 756 766 11 SRKYTSFPWLL 648 B*2702 80 1.92 152 22 757 792 756 766 11 SRKYTSFPWLL 648 B*3901 26 1.92 50 22 757 792 757 766 10 RKYTSFPWLL 649 B*1302 8 1.92 16 22 757 792 757 766 10 RKYTSFPWLL 649 B*1402 63 1.92 120 22 757 792 757 766 10 RKYTSFPWLL 649 B*2702 70 1.92 134 22 757 792 757 766 10 RKYTSFPWLL 649 B*3901 17 1.92 32 22 757 792 757 766 10 RKYTSFPWLL 649 B*4801 75 1.92 144 22 757 792 758 766 9 KYTSFPWLL 650 A*2301 97 1.92 185 22 757 792 758 766 9 KYTSFPWLL 650 A*2402 96 1.92 185 22 757 792 759 766 8 YTSFPWLL 651 A*0101 57 1.92 108 22 757 792 759 766 8 YTSFPWLL 651 A*2601 18 1.92 34 22 757 792 759 766 8 YTSFPWLL 651 B*5801 5 1.92 10 22 757 792 757 767 11 RKYTSFPWLLG 652 B*2705 48 0.64 31 22 757 792 758 767 10 KYTSFPWLLG 653 A*3201 11 0.64 7 22 757 792 759 767 9 YTSFPWLLG 654 A*0101 9 0.64 6 22 757 792 762 769 8 FPWLLGCT 655 B*3501 65 0.19 13 22 757 792 762 769 8 FPWLLGCT 655 B*3503 8 0.19 2 22 757 792 762 769 8 FPWLLGCT 655 B*5101 35 0.19 7 22 757 792 762 769 8 FPWLLGCT 655 B*5501 66 0.19 13 22 757 792 762 769 8 FPWLLGCT 655 B*5601 85 0.19 16 22 757 792 762 770 9 FPWLLGCTA 656 B*1402 14 1.76 25 22 757 792 762 770 9 FPWLLGCTA 656 B*3501 39 1.76 68 22 757 792 762 770 9 FPWLLGCTA 656 B*3503 88 1.76 155 22 757 792 762 770 9 FPWLLGCTA 656 B*5101 33 1.76 59 22 757 792 762 771 10 FPWLLGCTAN 657 B*0702 7 0.39 3 22 757 792 762 771 10 FPWLLGCTAN 657 B*3501 79 0.39 31 22 757 792 762 771 10 FPWLLGCTAN 657 B*3503 24 0.39 9 22 757 792 762 771 10 FPWLLGCTAN 657 B*5101 57 0.39 22 22 757 792 762 771 10 FPWLLGCTAN 657 B*5301 52 0.39 20 22 757 792 762 771 10 FPWLLGCTAN 657 B*5501 52 0.39 20 22 757 792 762 771 10 FPWLLGCTAN 657 B*5601 69 0.39 27 22 757 792 762 772 11 FPWLLGCTANW 658 B*1402 55 1.72 94 22 757 792 762 772 11 FPWLLGCTANW 658 B*1801 48 1.72 82 22 757 792 762 772 11 FPWLLGCTANW 658 B*3501 93 1.72 161 22 757 792 762 772 11 FPWLLGCTANW 658 B*3503 81 1.72 140 22 757 792 762 772 11 FPWLLGCTANW 658 B*3801 63 1.72 109 22 757 792 762 772 11 FPWLLGCTANW 658 B*5101 87 1.72 149 22 757 792 762 772 11 FPWLLGCTANW 658 B*5501 8 1.72 14 22 757 792 762 772 11 FPWLLGCTANW 658 B*5601 50 1.72 86 22 757 792 763 772 10 PWLLGCTANW 659 A*2301 67 1.72 116 22 757 792 763 772 10 PWLLGCTANW 659 A*2402 32 1.72 54 22 757 792 764 772 9 WLLGCTANW 660 B*5701 26 1.72 44 22 757 792 764 773 10 WLLGcTANWI 661 A*0201 91 0.22 20 22 757 792 765 773 9 LLGCTANWI 662 A*0201 71 0.22 15 22 757 792 764 774 11 WLLGCTANWIL 663 B*3801 18 1.41 26 22 757 792 764 774 11 WLLGCTANWIL 663 B*3901 74 1.41 104 22 757 792 764 774 11 WLLGCTANWIL 663 B*4801 40 1.41 57 22 757 792 765 774 10 LLGCtANWIL 664 A*0201 64 1.41 90 22 757 792 765 775 11 LLGCTANWILR 665 A*7401 30 1.01 31 22 757 792 766 775 10 LGCTANWILR 666 A*3201 33 1.01 34 22 757 792 768 775 8 CTANWILR 667 A*1101 72 1.01 72 22 757 792 768 775 8 CTANWILR 667 A*3101 53 1.01 54 22 757 792 768 775 8 CTANWILR 667 A*3303 79 1.01 80 22 757 792 768 775 8 CTANWILR 667 A*6801 94 1.01 95 22 757 792 768 775 8 CTANWILR 667 A*7401 74 1.01 75 22 757 792 769 779 11 TANWILRGTSF 668 B*1502 33 1.20 40 22 757 792 769 779 11 TANWILRGTSF 668 B*3501 11 1.20 13 22 757 792 769 779 11 TANWILRGTSF 668 B*4601 25 1.20 29 22 757 792 769 779 11 TANWILRGTSF 668 B*5802 20 1.20 24 22 757 792 770 779 10 ANWILRGTSF 669 B*4402 8 1.20 9 22 757 792 771 779 9 NWILRGTSF 670 A*2301 2 1.20 2 22 757 792 771 779 9 NWILRGTSF 670 A*2402 30 1.20 36 22 757 792 772 779 8 WILRGTSF 671 B*0801 7 1.20 8 22 757 792 772 779 8 WILRGTSF 671 B*1501 52 1.20 62 22 757 792 772 779 8 WILRGTSF 671 B*1502 81 1.20 97 22 757 792 772 779 8 WILRGTSF 671 B*1525 63 1.20 75 22 757 792 772 779 8 WILRGTSF 671 B*4601 39 1.20 47 22 757 792 772 780 9 WILRGTSFV 672 A*0201 100 1.19 119 22 757 792 772 780 9 WILRGTSFV 672 A*0206 69 1.19 82 22 757 792 771 781 11 NWILRGTSFVY 673 A*2902 51 1.69 86 22 757 792 771 781 11 NWILRGTSFVY 673 B*1801 24 1.69 40 22 757 792 772 781 10 WILRGTSFVY 674 B*1502 59 1.69 100 22 757 792 772 781 10 WILRGTSFVY 674 B*1525 8 1.69 14 22 757 792 772 781 10 WILRGTSFVY 674 B*4601 2 1.69 3 22 757 792 773 781 9 ILRGTSFVY 675 A*0301 23 1.69 39 22 757 792 773 781 9 ILRGTSFVY 675 A*2902 63 1.69 108 22 757 792 773 781 9 ILRGTSFVY 675 A*3002 72 1.69 122 22 757 792 773 781 9 ILRGTSFVY 675 B*1501 83 1.69 140 22 757 792 773 781 9 ILRGTSFVY 675 B*1525 69 1.69 118 22 757 792 774 781 8 LRGTSFVY 676 B*2702 23 1.69 39 22 757 792 774 781 8 LRGTSFVY 676 B*2705 37 1.69 63 22 757 792 773 782 10 ILRGTSFVYV 677 A*0201 71 1.67 119 22 757 792 776 785 10 GTSFVYVPSA 678 A*3001 73 1.35 98 22 757 792 776 785 10 GTSFVYVPSA 678 B*5701 45 1.35 61 22 757 792 778 786 9 SFVYVPSAL 679 B*1402 7 1.57 11 22 757 792 779 786 8 FVYVPSAL 680 A*2501 27 1.57 42 22 757 792 779 786 8 FVYVPSAL 680 B*0801 5 1.57 8 22 757 792 779 786 8 FVYVPSAL 680 B*1402 75 1.57 118 22 757 792 779 786 8 FVYVPSAL 680 B*1502 54 1.57 85 22 757 792 779 786 8 FVYVPSAL 680 B*3503 41 1.57 64 22 757 792 779 786 8 FVYVPSAL 680 B*3801 41 1.57 64 22 757 792 779 786 8 FVYVPSAL 680 B*3901 73 1.57 114 22 757 792 779 786 8 FVYVPSAL 680 B*4601 77 1.57 121 22 757 792 779 786 8 FVYVPSAL 680 B*5501 45 1.57 71 22 757 792 779 786 8 FVYVPSAL 680 B*5601 24 1.57 38 22 757 792 781 788 8 YVPSALNP 681 A*0206 73 0.38 27 22 757 792 779 789 11 FVYVPSALNPA 682 A*6802 15 0.68 10 22 757 792 779 789 11 FVYVPSALNPA 682 B*4601 67 0.68 46 22 757 792 779 789 11 FVYVPSALNPA 682 B*5501 65 0.68 44 22 757 792 779 789 11 FVYVPSALNPA 682 B*5601 74 0.68 51 22 757 792 781 789 9 YVPSALNPA 683 A*0206 42 0.68 28 22 757 792 782 789 8 VPSALNPA 684 B*0702 22 0.68 15 22 757 792 782 789 8 VPSALNPA 684 B*3503 1 0.68 1 22 757 792 782 789 8 VPSALNPA 684 B*5101 5 0.68 3 22 757 792 782 789 8 VPSALNPA 684 B*5501 80 0.68 55 22 757 792 782 789 8 VPSALNPA 684 B*5601 91 0.68 62 22 757 792 781 790 10 YVPSALNPAD 685 A*3001 14 0.18 3 22 757 792 Cumulative Class I-BCI score: 6817 754 762 9 VLSRKYTSF 638 B*0801 68 1.77 120 23 754 789 754 762 9 VLSRKYTSF 638 B*1501 17 1.77 30 23 754 789 755 762 8 LSRKYTSF 639 B*0801 61 1.77 108 23 754 789 755 762 8 LSRKYTSF 639 B*1501 98 1.77 174 23 754 789 755 762 8 LSRKYTSF 639 B*1502 85 1.77 150 23 754 789 755 762 8 LSRKYTSF 639 B*1525 81 1.77 144 23 754 789 755 762 8 LSRKYTSF 639 B*4601 59 1.77 104 23 754 789 755 762 8 LSRKYTSF 639 B*5701 61 1.77 107 23 754 789 755 762 8 LSRKYTSF 639 B*5802 46 1.77 82 23 754 789 754 764 11 VLSRKYTSFPW 640 A*3201 17 0.99 16 23 754 789 754 764 11 VLSRKYTSFPW 640 B*5701 55 0.99 54 23 754 789 754 764 11 VLSRKYTSFPW 640 B*5801 56 0.99 55 23 754 789 754 764 11 VLSRKYTSFPW 640 B*5802 22 0.99 21 23 754 789 755 764 10 LSRKYTSFPW 641 B*1525 10 0.99 10 23 754 789 755 764 10 LSRKYTSFPW 641 B*5802 96 0.99 94 23 754 789 756 764 9 SRKYTSFPW 642 B*2702 81 0.99 80 23 754 789 757 764 8 RKYTSFPW 643 B*1301 52 0.99 51 23 754 789 757 764 8 RKYTSFPW 643 B*2702 94 0.99 93 23 754 789 757 764 8 RKYTSFPW 643 B*4402 4 0.99 4 23 754 789 757 764 8 RKYTSFPW 643 B*4403 12 0.99 12 23 754 789 757 764 8 RKYTSFPW 643 B*5701 3 0.99 3 23 754 789 757 764 8 RKYTSFPW 643 B*5802 12 0.99 11 23 754 789 755 765 11 LSRKYTSFPWL 644 A*3001 36 1.24 45 23 754 789 755 765 11 LSRKYTSFPWL 644 B*0801 36 1.24 44 23 754 789 756 765 10 SRKYTSFPWL 645 A*3001 21 1.24 26 23 754 789 756 765 10 SRKYTSFPWL 645 B*1402 24 1.24 30 23 754 789 756 765 10 SRKYTSFPWL 645 B*2702 46 1.24 57 23 754 789 756 765 10 SRKYTSFPWL 645 B*2705 10 1.24 13 23 754 789 757 765 9 RKYTSFPWL 646 B*1402 8 1.24 10 23 754 789 757 765 9 RKYTSFPWL 646 B*2702 4 1.24 4 23 754 789 757 765 9 RKYTSFPWL 646 B*4801 87 1.24 108 23 754 789 758 765 8 KYTSFPWL 647 A*2301 81 1.24 101 23 754 789 758 765 8 KYTSFPWL 647 A*2402 77 1.24 96 23 754 789 756 766 11 SRKYTSFPWLL 648 B*1402 64 1.92 122 23 754 789 756 766 11 SRKYTSFPWLL 648 B*2702 80 1.92 152 23 754 789 756 766 11 SRKYTSFPWLL 648 B*3901 26 1.92 50 23 754 789 757 766 10 RKYTSFPWLL 649 B*1302 8 1.92 16 23 754 789 757 766 10 RKYTSFPWLL 649 B*1402 63 1.92 120 23 754 789 757 766 10 RKYTSFPWLL 649 B*2702 70 1.92 134 23 754 789 757 766 10 RKYTSFPWLL 649 B*3901 17 1.92 32 23 754 789 757 766 10 RKYTSFPWLL 649 B*4801 75 1.92 144 23 754 789 758 766 9 KYTSFPWLL 650 A*2301 97 1.92 185 23 754 789 758 766 9 KYTSFPWLL 650 A*2402 96 1.92 185 23 754 789 759 766 8 YTSFPWLL 651 A*0101 57 1.92 108 23 754 789 759 766 8 YTSFPWLL 651 A*2601 18 1.92 34 23 754 789 759 766 8 YTSFPWLL 651 B*5801 5 1.92 10 23 754 789 757 767 11 RKYTSFPWLLG 652 B*2705 48 0.64 31 23 754 789 758 767 10 KYTSFPWLLG 653 A*3201 11 0.64 7 23 754 789 759 767 9 YTSFPWLLG 654 A*0101 9 0.64 6 23 754 789 762 769 8 FPWLLGCT 655 B*3501 65 0.19 13 23 754 789 762 769 8 FPWLLGCT 655 B*3503 8 0.19 2 23 754 789 762 769 8 FPWLLGCT 655 B*5101 35 0.19 7 23 754 789 762 769 8 FPWLLGCT 655 B*5501 66 0.19 13 23 754 789 762 769 8 FPWLLGCT 655 B*5601 85 0.19 16 23 754 789 762 770 9 FPWLLGCTA 656 B*1402 14 1.76 25 23 754 789 762 770 9 FPWLLGCTA 656 B*3501 39 1.76 68 23 754 789 762 770 9 FPWLLGCTA 656 B*3503 88 1.76 155 23 754 789 762 770 9 FPWLLGCTA 656 B*5101 33 1.76 59 23 754 789 762 771 10 FPWLLGCTAN 657 B*0702 7 0.39 3 23 754 789 762 771 10 FPWLLGCTAN 657 B*3501 79 0.39 31 23 754 789 762 771 10 FPWLLGCTAN 657 B*3503 24 0.39 9 23 754 789 762 771 10 FPWLLGCTAN 657 B*5101 57 0.39 22 23 754 789 762 771 10 FPWLLGCTAN 657 B*5301 52 0.39 20 23 754 789 762 771 10 FPWLLGCTAN 657 B*5501 52 0.39 20 23 754 789 762 771 10 FPWLLGCTAN 657 B*5601 69 0.39 27 23 754 789 762 772 11 FPWLLGCTANW 658 B*1402 55 1.72 94 23 754 789 762 772 11 FPWLLGCTANW 658 B*1801 48 1.72 82 23 754 789 762 772 11 FPWLLGCTANW 658 B*3501 93 1.72 161 23 754 789 762 772 11 FPWLLGCTANW 658 B*3503 81 1.72 140 23 754 789 762 772 11 FPWLLGCTANW 658 B*3801 63 1.72 109 23 754 789 762 772 11 FPWLLGCTANW 658 B*5101 87 1.72 149 23 754 789 762 772 11 FPWLLGCTANW 658 B*5501 8 1.72 14 23 754 789 762 772 11 FPWLLGCTANW 658 B*5601 50 1.72 86 23 754 789 763 772 10 PWLLGCTANW 659 A*2301 67 1.72 116 23 754 789 763 772 10 PWLLGCTANW 659 A*2402 32 1.72 54 23 754 789 764 772 9 WLLGCTANW 660 B*5701 26 1.72 44 23 754 789 764 773 10 WLLGcTANWI 661 A*0201 91 0.22 20 23 754 789 765 773 9 LLGCTANWI 662 A*0201 71 0.22 15 23 754 789 764 774 11 WLLGCTANWIL 663 B*3801 18 1.41 26 23 754 789 764 774 11 WLLGCTANWIL 663 B*3901 74 1.41 104 23 754 789 764 774 11 WLLGCTANWIL 663 B*4801 40 1.41 57 23 754 789 765 774 10 LLGCtANWIL 664 A*0201 64 1.41 90 23 754 789 765 775 11 LLGCTANWILR 665 A*7401 30 1.01 31 23 754 789 766 775 10 LGCTANWILR 666 A*3201 33 1.01 34 23 754 789 768 775 8 CTANWILR 667 A*1101 72 1.01 72 23 754 789 768 775 8 CTANWILR 667 A*3101 53 1.01 54 23 754 789 768 775 8 CTANWILR 667 A*3303 79 1.01 80 23 754 789 768 775 8 CTANWILR 667 A*6801 94 1.01 95 23 754 789 768 775 8 CTANWILR 667 A*7401 74 1.01 75 23 754 789 769 779 11 TANWILRGTSF 668 B*1502 33 1.20 40 23 754 789 769 779 11 TANWILRGTSF 668 B*3501 11 1.20 13 23 754 789 769 779 11 TANWILRGTSF 668 B*4601 25 1.20 29 23 754 789 769 779 11 TANWILRGTSF 668 B*5802 20 1.20 24 23 754 789 770 779 10 ANWILRGTSF 669 B*4402 8 1.20 9 23 754 789 771 779 9 NWILRGTSF 670 A*2301 2 1.20 2 23 754 789 771 779 9 NWILRGTSF 670 A*2402 30 1.20 36 23 754 789 772 779 8 WILRGTSF 671 B*0801 7 1.20 8 23 754 789 772 779 8 WILRGTSF 671 B*1501 52 1.20 62 23 754 789 772 779 8 WILRGTSF 671 B*1502 81 1.20 97 23 754 789 772 779 8 WILRGTSF 671 B*1525 63 1.20 75 23 754 789 772 779 8 WILRGTSF 671 B*4601 39 1.20 47 23 754 789 772 780 9 WILRGTSFV 672 A*0201 100 1.19 119 23 754 789 772 780 9 WILRGTSFV 672 A*0206 69 1.19 82 23 754 789 771 781 11 NWILRGTSFVY 673 A*2902 51 1.69 86 23 754 789 771 781 11 NWILRGTSFVY 673 B*1801 24 1.69 40 23 754 789 772 781 10 WILRGTSFVY 674 B*1502 59 1.69 100 23 754 789 772 781 10 WILRGTSFVY 674 B*1525 8 1.69 14 23 754 789 772 781 10 WILRGTSFVY 674 B*4601 2 1.69 3 23 754 789 773 781 9 ILRGTSFVY 675 A*0301 23 1.69 39 23 754 789 773 781 9 ILRGTSFVY 675 A*2902 63 1.69 108 23 754 789 773 781 9 ILRGTSFVY 675 A*3002 72 1.69 122 23 754 789 773 781 9 ILRGTSFVY 675 B*1501 83 1.69 140 23 754 789 773 781 9 ILRGTSFVY 675 B*1525 69 1.69 118 23 754 789 774 781 8 LRGTSFVY 676 B*2702 23 1.69 39 23 754 789 774 781 8 LRGTSFVY 676 B*2705 37 1.69 63 23 754 789 773 782 10 ILRGTSFVYV 677 A*0201 71 1.67 119 23 754 789 776 785 10 GTSFVYVPSA 678 A*3001 73 1.35 98 23 754 789 776 785 10 GTSFVYVPSA 678 B*5701 45 1.35 61 23 754 789 778 786 9 SFVYVPSAL 679 B*1402 7 1.57 11 23 754 789 779 786 8 FVYVPSAL 680 A*2501 27 1.57 42 23 754 789 779 786 8 FVYVPSAL 680 B*0801 5 1.57 8 23 754 789 779 786 8 FVYVPSAL 680 B*1402 75 1.57 118 23 754 789 779 786 8 FVYVPSAL 680 B*1502 54 1.57 85 23 754 789 779 786 8 FVYVPSAL 680 B*3503 41 1.57 64 23 754 789 779 786 8 FVYVPSAL 680 B*3801 41 1.57 64 23 754 789 779 786 8 FVYVPSAL 680 B*3901 73 1.57 114 23 754 789 779 786 8 FVYVPSAL 680 B*4601 77 1.57 121 23 754 789 779 786 8 FVYVPSAL 680 B*5501 45 1.57 71 23 754 789 779 786 8 FVYVPSAL 680 B*5601 24 1.57 38 23 754 789 781 788 8 YVPSALNP 681 A*0206 73 0.38 27 23 754 789 779 789 11 FVYVPSALNPA 682 A*6802 15 0.68 10 23 754 789 779 789 11 FVYVPSALNPA 682 B*4601 67 0.68 46 23 754 789 779 789 11 FVYVPSALNPA 682 B*5501 65 0.68 44 23 754 789 779 789 11 FVYVPSALNPA 682 B*5601 74 0.68 51 23 754 789 781 789 9 YVPSALNPA 683 A*0206 42 0.68 28 23 754 789 782 789 8 VPSALNPA 684 B*0702 22 0.68 15 23 754 789 782 789 8 VPSALNPA 684 B*3503 1 0.68 1 23 754 789 782 789 8 VPSALNPA 684 B*5101 5 0.68 3 23 754 789 782 789 8 VPSALNPA 684 B*5501 80 0.68 55 23 754 789 782 789 8 VPSALNPA 684 B*5601 91 0.68 62 23 754 789 Cumulative Class I-BCI score: 8553 “Start” and “End” are relative to the amino acid sequence of HBV polymerase as depicted in SEQ ID NO: 1 ^(A) Peptide amino acid sequence. Each HLA class I binding peptide of HBV polymerase is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods (Examples section). ^(C)C-score. See Material and Methods (Examples section). ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 4b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV polymerase protein. HLA class II binding peptides in SLP sequences derived from HBV Polymerase SEQ HLA- Class ID DRB1 II-B Peptide of invention (SLP) Start End Sequence ^(A) NO: molecule score^(B) SLP# SLP Start SLP End 1 15 MPLSYQHFRKLLLLD 686 *0701 79 1 1 30 1 15 MPLSYQHFRKLLLLD 686 *1101 86 1 1 30 1 15 MPLSYQHFRKLLLLD 686 *1501 9 1 1 30 2 16 PLSYQHFRKLLLLDD 687 *0701 40 1 1 30 2 16 PLSYQHFRKLLLLDD 687 *1101 84 1 1 30 2 16 PLSYQHFRKLLLLDD 687 *1501 4 1 1 30 3 17 LSYQHFRKLLLLDDG 688 *0701 9 1 1 30 3 17 LSYQHFRKLLLLDDG 688 *1101 83 1 1 30 3 17 LSYQHFRKLLLLDDG 688 *1501 3 1 1 30 4 18 SYQHFRKLLLLDDGT 689 *1101 81 1 1 30 5 19 YQHFRKLLLLDDGTE 690 *1101 80 1 1 30 6 20 QHFRKLLLLDDGTEA 691 *0301 31 1 1 30 6 20 QHFRKLLLLDDGTEA 691 *1101 56 1 1 30 7 21 HFRKLLLLDDGTEAG 692 *0301 30 1 1 30 8 22 FRKLLLLDDGTEAGP 693 *0301 29 1 1 30 9 23 RKLLLLDDGTEAGPL 694 *0301 27 1 1 30 10 24 KLLLLDDGTEAGPLE 695 *0301 26 1 1 30 11 25 LLLLDDGTEAGPLEE 696 *0301 24 1 1 30 Cumulative Class II-B score^(C): 780 55 69 THKVGNFTGLYSSTV 697 *0101 14 2 52 86 55 69 THKVGNFTGLYSSTV 697 *1501 54 2 52 86 56 70 HKVGNFTGLYSSTVP 698 *0101 10 2 52 86 56 70 HKVGNFTGLYSSTVP 698 *1501 51 2 52 86 57 71 KVGNFTGLYSSTVPI 699 *0101 64 2 52 86 57 71 KVGNFTGLYSSTVPI 699 *0105 78 2 52 86 57 71 KVGNFTGLYSSTVPI 699 *0107 78 2 52 86 57 71 KVGNFTGLYSSTVPI 699 *0401 11 2 52 86 57 71 KVGNFTGLYSSTVPI 699 *0701 26 2 52 86 57 71 KVGNFTGLYSSTVPI 699 *1501 47 2 52 86 58 72 VGNFTGLYSSTVPIF 700 *0101 93 2 52 86 58 72 VGNFTGLYSSTVPIF 700 *0105 88 2 52 86 58 72 VGNFTGLYSSTVPIF 700 *0107 88 2 52 86 58 72 VGNFTGLYSSTVPIF 700 *0301 14 2 52 86 58 72 VGNFTGLYSSTVPIF 700 *0401 23 2 52 86 58 72 VGNFTGLYSSTVPIF 700 *0701 34 2 52 86 58 72 VGNFTGLYSSTVPIF 700 *1501 59 2 52 86 59 73 GNFTGLYSSTVPIFN 701 *0101 80 2 52 86 59 73 GNFTGLYSSTVPIFN 701 *0105 55 2 52 86 59 73 GNFTGLYSSTVPIFN 701 *0107 55 2 52 86 59 73 GNFTGLYSSTVPIFN 701 *0301 16 2 52 86 59 73 GNFTGLYSSTVPIFN 701 *0401 24 2 52 86 59 73 GNFTGLYSSTVPIFN 701 *0701 54 2 52 86 60 74 NFTGLYSSTVPIFNP 702 *0101 57 2 52 86 60 74 NFTGLYSSTVPIFNP 702 *0301 11 2 52 86 60 74 NFTGLYSSTVPIFNP 702 *0401 16 2 52 86 60 74 NFTGLYSSTVPIFNP 702 *0701 30 2 52 86 61 75 FTGLYSSTVPIFNPE 703 *0101 43 2 52 86 61 75 FTGLYSSTVPIFNPE 703 *0301 13 2 52 86 61 75 FTGLYSSTVPIFNPE 703 *0401 19 2 52 86 61 75 FTGLYSSTVPIFNPE 703 *0701 11 2 52 86 62 76 TGLYSSTVPIFNPEW 704 *0301 7 2 52 86 Cumulative Class II-B score: 1323 103 117 VNEKRRLKLIMPARF 705 *0101 47 3 103 135 103 117 VNEKRRLKLIMPARF 705 *0102 33 3 103 135 103 117 VNEKRRLKLIMPARF 705 *0104 8 3 103 135 103 117 VNEKRRLKLIMPARF 705 *0106 50 3 103 135 103 117 VNEKRRLKLIMPARF 705 *0301 36 3 103 135 103 117 VNEKRRLKLIMPARF 705 *0701 17 3 103 135 103 117 VNEKRRLKLIMPARF 705 *1301 7 3 103 135 103 117 VNEKRRLKLIMPARF 705 *1501 64 3 103 135 104 118 NEKRRLKLIMPARFY 706 *0101 53 3 103 135 104 118 NEKRRLKLIMPARFY 706 *0102 83 3 103 135 104 118 NEKRRLKLIMPARFY 706 *0104 78 3 103 135 104 118 NEKRRLKLIMPARFY 706 *0106 83 3 103 135 104 118 NEKRRLKLIMPARFY 706 *0701 27 3 103 135 104 118 NEKRRLKLIMPARFY 706 *1301 64 3 103 135 104 118 NEKRRLKLIMPARFY 706 *1501 76 3 103 135 105 119 EKRRLKLIMPARFYP 707 *0101 46 3 103 135 105 119 EKRRLKLIMPARFYP 707 *0102 93 3 103 135 105 119 EKRRLKLIMPARFYP 707 *0104 85 3 103 135 105 119 EKRRLKLIMPARFYP 707 *0106 85 3 103 135 105 119 EKRRLKLIMPARFYP 707 *0701 3 3 103 135 105 119 EKRRLKLIMPARFYP 707 *1101 8 3 103 135 105 119 EKRRLKLIMPARFYP 707 *1301 61 3 103 135 105 119 EKRRLKLIMPARFYP 707 *1501 71 3 103 135 106 120 KRRLKLIMPARFYPT 708 *0101 49 3 103 135 106 120 KRRLKLIMPARFYPT 708 *0102 100 3 103 135 106 120 KRRLKLIMPARFYPT 708 *0103 4 3 103 135 106 120 KRRLKLIMPARFYPT 708 *0104 100 3 103 135 106 120 KRRLKLIMPARFYPT 708 *0105 45 3 103 135 106 120 KRRLKLIMPARFYPT 708 *0106 93 3 103 135 106 120 KRRLKLIMPARFYPT 708 *0107 45 3 103 135 106 120 KRRLKLIMPARFYPT 708 *1101 25 3 103 135 106 120 KRRLKLIMPARFYPT 708 *1301 71 3 103 135 106 120 KRRLKLIMPARFYPT 708 *1501 73 3 103 135 107 121 RRLKLIMPARFYPTH 709 *0101 44 3 103 135 107 121 RRLKLIMPARFYPTH 709 *0102 80 3 103 135 107 121 RRLKLIMPARFYPTH 709 *0104 88 3 103 135 107 121 RRLKLIMPARFYPTH 709 *0106 78 3 103 135 107 121 RRLKLIMPARFYPTH 709 *1301 32 3 103 135 107 121 RRLKLIMPARFYPTH 709 *1501 69 3 103 135 108 122 RLKLIMPARFYPTHT 710 *0102 53 3 103 135 108 122 RLKLIMPARFYPTHT 710 *0104 53 3 103 135 108 122 RLKLIMPARFYPTHT 710 *0106 60 3 103 135 108 122 RLKLIMPARFYPTHT 710 *1501 41 3 103 135 109 123 LKLIMPARFYPTHTK 711 *1501 40 3 103 135 111 125 LIMPARFYPTHTKYL 712 *0701 93 3 103 135 112 126 IMPARFYPTHTKYLP 713 *0701 91 3 103 135 113 127 MPARFYPTHTKYLPL 714 *0701 96 3 103 135 114 128 PARFYPTHTKYLPLD 715 *0701 94 3 103 135 115 129 ARFYPTHTKYLPLDK 716 *0701 90 3 103 135 116 130 RFYPTHTKYLPLDKG 717 *0701 86 3 103 135 117 131 FYPTHTKYLPLDKGI 718 *0701 81 3 103 135 121 135 HTKYLPLDKGIKPYY 719 *1101 23 3 103 135 Cumulative Class II-B score: 3070 121 135 HTKYLPLDKGIKPYY 719 *1101 23 4 118 150 122 136 TKYLPLDKGIKPYYP 720 *1101 21 4 118 150 130 144 GIKPYYPDQVVNHYF 721 *0401 26 4 118 150 131 145 IKPYYPDQVVNHYFQ 722 *0401 51 4 118 150 132 146 KPYYPDQVVNHYFQT 723 *0401 21 4 118 150 Cumulative Class II-B score: 143 139 153 VVNHYFQTRHYLHTL 726 *1101 87 5 139 177 139 153 VVNHYFQTRHYLHTL 726 *1501 70 5 139 177 140 154 VNHYFQTRHYLHTLW 727 *0701 70 5 139 177 140 154 VNHYFQTRHYLHTLW 727 *1101 76 5 139 177 140 154 VNHYFQTRHYLHTLW 727 *1501 58 5 139 177 141 155 NHYFQTRHYLHTLWK 728 *0701 40 5 139 177 141 155 NHYFQTRHYLHTLWK 728 *1101 79 5 139 177 141 155 NHYFQTRHYLHTLWK 728 *1501 28 5 139 177 142 156 HYFQTRHYLHTLWKA 729 *1101 54 5 139 177 142 156 HYFQTRHYLHTLWKA 729 *1501 30 5 139 177 143 157 YFQTRHYLHTLWKAG 730 *1101 24 5 139 177 144 158 FQTRHYLHTLWKAGI 731 *1101 55 5 139 177 144 158 FQTRHYLHTLWKAGI 731 *1501 5 5 139 177 145 159 QTRHYLHTLWKAGIL 732 *1101 78 5 139 177 145 159 QTRHYLHTLWKAGIL 732 *1501 38 5 139 177 146 160 TRHYLHTLWKAGILY 733 *1101 88 5 139 177 146 160 TRHYLHTLWKAGILY 733 *1501 45 5 139 177 147 161 RHYLHTLWKAGILYK 734 *1101 85 5 139 177 147 161 RHYLHTLWKAGILYK 734 *1501 40 5 139 177 148 162 HYLHTLWKAGILYKR 735 *1101 50 5 139 177 154 168 WKAGILYKRETTRSA 736 *0401 81 5 139 177 155 169 KAGILYKRETTRSAS 737 *0401 83 5 139 177 156 170 AGILYKRETTRSASF 738 *0401 84 5 139 177 157 171 GILYKRETTRSASFC 739 *0401 80 5 139 177 158 172 ILYKRETTRSASFCG 740 *0401 79 5 139 177 159 173 LYKRETTRSASFCGS 741 *0401 14 5 139 177 Cumulative Class II-B score: 1519 143 157 YFQTRHYLHTLWKAG 730 *1101 24 6 143 177 144 158 FQTRHYLHTLWKAGI 731 *1101 55 6 143 177 144 158 FQTRHYLHTLWKAGI 731 *1501 5 6 143 177 145 159 QTRHYLHTLWKAGIL 732 *1101 78 6 143 177 145 159 QTRHYLHTLWKAGIL 732 *1501 38 6 143 177 146 160 TRHYLHTLWKAGILY 733 *1101 88 6 143 177 146 160 TRHYLHTLWKAGILY 733 *1501 45 6 143 177 147 161 RHYLHTLWKAGILYK 734 *1101 85 6 143 177 147 161 RHYLHTLWKAGILYK 734 *1501 40 6 143 177 148 162 HYLHTLWKAGILYKR 735 *1101 50 6 143 177 154 168 WKAGILYKRETTRSA 736 *0401 81 6 143 177 155 169 KAGILYKRETTRSAS 737 *0401 83 6 143 177 156 170 AGILYKRETTRSASF 738 *0401 84 6 143 177 157 171 GILYKRETTRSASFC 739 *0401 80 6 143 177 158 172 ILYKRETTRSASFCG 740 *0401 79 6 143 177 159 173 LYKRETTRSASFCGS 741 *0401 14 6 143 177 Cumulative Class II-B score: 928 137 151 DQVVNHYFQTRHYLH 724 *0701 53 7 137 170 137 151 DQVVNHYFQTRHYLH 724 *1101 75 7 137 170 137 151 DQVVNHYFQTRHYLH 724 *1501 63 7 137 170 138 152 QVVNHYFQTRHYLHT 725 *0701 63 7 137 170 138 152 QVVNHYFQTRHYLHT 725 *1101 59 7 137 170 138 152 QVVNHYFQTRHYLHT 725 *1501 73 7 137 170 139 153 VVNHYFQTRHYLHTL 726 *0701 88 7 137 170 139 153 VVNHYFQTRHYLHTL 726 *1101 87 7 137 170 139 153 VVNHYFQTRHYLHTL 726 *1501 70 7 137 170 140 154 VNHYFQTRHYLHTLW 727 *0701 70 7 137 170 140 154 VNHYFQTRHYLHTLW 727 *1101 76 7 137 170 140 154 VNHYFQTRHYLHTLW 727 *1501 58 7 137 170 141 155 NHYFQTRHYLHTLWK 728 *0701 40 7 137 170 141 155 NHYFQTRHYLHTLWK 728 *1101 79 7 137 170 141 155 NHYFQTRHYLHTLWK 728 *1501 28 7 137 170 142 156 HYFQTRHYLHTLWKA 729 *1101 54 7 137 170 142 156 HYFQTRHYLHTLWKA 729 *1501 30 7 137 170 143 157 YFQTRHYLHTLWKAG 730 *1101 24 7 137 170 144 158 FQTRHYLHTLWKAGI 731 *1101 55 7 137 170 144 158 FQTRHYLHTLWKAGI 731 *1501 5 7 137 170 145 159 QTRHYLHTLWKAGIL 732 *1101 78 7 137 170 145 159 QTRHYLHTLWKAGIL 732 *1501 38 7 137 170 146 160 TRHYLHTLWKAGILY 733 *1101 88 7 137 170 146 160 TRHYLHTLWKAGILY 733 *1501 45 7 137 170 147 161 RHYLHTLWKAGILYK 734 *1101 85 7 137 170 147 161 RHYLHTLWKAGILYK 734 *1501 40 7 137 170 148 162 HYLHTLWKAGILYKR 735 *1101 50 7 137 170 154 168 WKAGILYKRETTRSA 736 *0401 81 7 137 170 155 169 KAGILYKRETTRSAS 737 *0401 83 7 137 170 156 170 AGILYKRETTRSASF 738 *0401 84 7 137 170 Cumulative Class II-B score: 1817 324 338 SCWWLQFRNSKPCSE 742 *0401 3 8 316 347 385 399 TAESRLVVDFSQFSR 743 *0301 97 9 385 417 386 400 AESRLVVDFSQFSRG 744 *0301 87 9 385 417 387 401 ESRLVVDFSQFSRGI 745 *0301 96 9 385 417 388 402 SRLVVDFSQFSRGIS 746 *0301 94 9 385 417 389 403 RLVVDFSQFSRGISR 747 *0301 77 9 385 417 390 404 LVVDFSQFSRGISRV 748 *0301 76 9 385 417 Cumulative Class II-B score: 527 421 435 LSSNLSWLSLDVSAA 749 *0401 27 10 419 456 422 436 SSNLSWLSLDVSAAF 750 *0301 57 10 419 456 422 436 SSNLSWLSLDVSAAF 750 *0401 71 10 419 456 423 437 SNLSWLSLDVSAAFY 751 *0301 56 10 419 456 423 437 SNLSWLSLDVSAAFY 751 *0401 70 10 419 456 424 438 NLSWLSLDVSAAFYH 752 *0301 54 10 419 456 424 438 NLSWLSLDVSAAFYH 752 *0401 69 10 419 456 425 439 LSWLSLDVSAAFYHI 753 *0301 53 10 419 456 425 439 LSWLSLDVSAAFYHI 753 *0401 67 10 419 456 425 439 LSWLSLDVSAAFYHI 753 *1301 18 10 419 456 426 440 SWLSLDVSAAFYHIP 754 *0301 51 10 419 456 426 440 SWLSLDVSAAFYHIP 754 *0401 66 10 419 456 427 441 WLSLDVSAAFYHIPL 755 *0301 50 10 419 456 427 441 WLSLDVSAAFYHIPL 755 *0401 17 10 419 456 428 442 LSLDVSAAFYHIPLH 756 *0301 49 10 419 456 432 446 VSAAFYHIPLHPAAM 757 *0101 8 10 419 456 432 446 VSAAFYHIPLHPAAM 757 *0105 8 10 419 456 432 446 VSAAFYHIPLHPAAM 757 *0107 8 10 419 456 433 447 SAAFYHIPLHPAAMP 758 *0101 35 10 419 456 433 447 SAAFYHIPLHPAAMP 758 *0105 35 10 419 456 433 447 SAAFYHIPLHPAAMP 758 *0107 35 10 419 456 433 447 SAAFYHIPLHPAAMP 758 *1101 3 10 419 456 434 448 AAFYHIPLHPAAMPH 759 *0101 13 10 419 456 434 448 AAFYHIPLHPAAMPH 759 *0105 13 10 419 456 434 448 AAFYHIPLHPAAMPH 759 *0107 13 10 419 456 Cumulative Class II-B score: 943 422 436 SSNLSWLSLDVSAAF 750 *0301 57 11 422 459 422 436 SSNLSWLSLDVSAAF 750 *0401 71 11 422 459 423 437 SNLSWLSLDVSAAFY 751 *0301 56 11 422 459 423 437 SNLSWLSLDVSAAFY 751 *0401 70 11 422 459 424 438 NLSWLSLDVSAAFYH 752 *0301 54 11 422 459 424 438 NLSWLSLDVSAAFYH 752 *0401 69 11 422 459 425 439 LSWLSLDVSAAFYHI 753 *0301 53 11 422 459 425 439 LSWLSLDVSAAFYHI 753 *0401 67 11 422 459 425 439 LSWLSLDVSAAFYHI 753 *1301 18 11 422 459 426 440 SWLSLDVSAAFYHIP 754 *0301 51 11 422 459 426 440 SWLSLDVSAAFYHIP 754 *0401 66 11 422 459 427 441 WLSLDVSAAFYHIPL 755 *0301 50 11 422 459 427 441 WLSLDVSAAFYHIPL 755 *0401 17 11 422 459 428 442 LSLDVSAAFYHIPLH 756 *0301 49 11 422 459 432 446 VSAAFYHIPLHPAAM 757 *0101 8 11 422 459 432 446 VSAAFYHIPLHPAAM 757 *0105 8 11 422 459 432 446 VSAAFYHIPLHPAAM 757 *0107 8 11 422 459 433 447 SAAFYHIPLHPAAMP 758 *0101 35 11 422 459 433 447 SAAFYHIPLHPAAMP 758 *0105 35 11 422 459 433 447 SAAFYHIPLHPAAMP 758 *0107 35 11 422 459 433 447 SAAFYHIPLHPAAMP 758 *1101 3 11 422 459 434 448 AAFYHIPLHPAAMPH 759 *0101 13 11 422 459 434 448 AAFYHIPLHPAAMPH 759 *0105 13 11 422 459 434 448 AAFYHIPLHPAAMPH 759 *0107 13 11 422 459 444 458 AAMPHLLIGSSGLSR 760 *0101 9 11 422 459 444 458 AAMPHLLIGSSGLSR 760 *0301 64 11 422 459 445 459 AMPHLLIGSSGLSRY 761 *0101 7 11 422 459 445 459 AMPFILLIGSSGLSRY 761 *0301 63 11 422 459 Cumulative Class II-B score: 1058 427 441 WLSLDVSAAFYHIPL 755 *0301 50 12 427 459 427 441 WLSLDVSAAFYHIPL 755 *0401 17 12 427 459 428 442 LSLDVSAAFYHIPLH 756 *0301 49 12 427 459 432 446 VSAAFYHIPLHPAAM 757 *0101 8 12 427 459 432 446 VSAAFYHIPLHPAAM 757 *0105 8 12 427 459 432 446 VSAAFYHIPLHPAAM 757 *0107 8 12 427 459 433 447 SAAFYHIPLHPAAMP 758 *0101 35 12 427 459 433 447 SAAFYHIPLHPAAMP 758 *0105 35 12 427 459 433 447 SAAFYHIPLHPAAMP 758 *0107 35 12 427 459 433 447 SAAFYHIPLHPAAMP 758 *1101 3 12 427 459 434 448 AAFYHIPLHPAAMPH 759 *0101 13 12 427 459 434 448 AAFYHIPLHPAAMPH 759 *0105 13 12 427 459 434 448 AAFYHIPLHPAAMPH 759 *0107 13 12 427 459 444 458 AAMPHLLIGSSGLSR 760 *0101 9 12 427 459 444 458 AAMPHLLIGSSGLSR 760 *0301 64 12 427 459 445 459 AMPHLLIGSSGLSRY 761 *0101 7 12 427 459 445 459 AMPHLLIGSSGLSRY 761 *0301 63 12 427 459 Cumulative Class II-B score: 426 483 497 SCSRQLYVSLMLLYK 762 *1101 94 13 481 514 484 498 CSRQLYVSLMLLYKT 763 *1101 93 13 481 514 484 498 CSRQLYVSLMLLYKT 763 *1501 20 13 481 514 485 499 SRQLYVSLMLLYKTY 764 *1101 91 13 481 514 485 499 SRQLYVSLMLLYKTY 764 *1501 10 13 481 514 486 500 RQLYVSLMLLYKTYG 765 *0301 47 13 481 514 486 500 RQLYVSLMLLYKTYG 765 *1101 100 13 481 514 486 500 RQLYVSLMLLYKTYG 765 *1301 21 13 481 514 486 500 RQLYVSLMLLYKTYG 765 *1501 23 13 481 514 487 501 QLYVSLMLLYKTYGW 766 *0301 10 13 481 514 487 501 QLYVSLMLLYKTYGW 766 *1101 99 13 481 514 487 501 QLYVSLMLLYKTYGW 766 *1301 20 13 481 514 487 501 QLYVSLMLLYKTYGW 766 *1501 61 13 481 514 488 502 LYVSLMLLYKTYGWK 767 *0301 9 13 481 514 488 502 LYVSLMLLYKTYGWK 767 *1101 97 13 481 514 488 502 LYVSLMLLYKTYGWK 767 *1301 19 13 481 514 488 502 LYVSLMLLYKTYGWK 767 *1501 60 13 481 514 489 503 YVSLMLLYKTYGWKL 768 *0701 100 13 481 514 489 503 YVSLMLLYKTYGWKL 768 *1101 96 13 481 514 489 503 YVSLMLLYKTYGWKL 768 *1301 17 13 481 514 489 503 YVSLMLLYKTYGWKL 768 *1501 99 13 481 514 490 504 VSLMLLYKTYGWKLH 769 *0701 99 13 481 514 490 504 VSLMLLYKTYGWKLH 769 *1301 16 13 481 514 490 504 VSLMLLYKTYGWKLH 769 *1501 100 13 481 514 491 505 SLMLLYKTYGWKLHL 770 *0701 97 13 481 514 491 505 SLMLLYKTYGWKLHL 770 *1301 14 13 481 514 491 505 SLMLLYKTYGWKLHL 770 *1501 97 13 481 514 492 506 LMLLYKTYGWKLHLY 771 *0106 3 13 481 514 492 506 LMLLYKTYGWKLHLY 771 *0701 89 13 481 514 492 506 LMLLYKTYGWKLHLY 771 *1101 5 13 481 514 492 506 LMLLYKTYGWKLHLY 771 *1301 13 13 481 514 492 506 LMLLYKTYGWKLHLY 771 *1501 77 13 481 514 493 507 MLLYKTYGWKLHLYS 772 *0701 87 13 481 514 493 507 MLLYKTYGWKLHLYS 772 *1101 9 13 481 514 493 507 MLLYKTYGWKLHLYS 772 *1501 66 13 481 514 494 508 LLYKTYGWKLHLYSH 773 *0701 84 13 481 514 494 508 LLYKTYGWKLHLYSH 773 *1101 7 13 481 514 494 508 LLYKTYGWKLHLYSH 773 *1501 85 13 481 514 495 509 LYKTYGWKLHLYSHP 774 *0701 74 13 481 514 495 509 LYKTYGWKLHLYSHP 774 *1101 6 13 481 514 495 509 LYKTYGWKLHLYSHP 774 *1501 13 13 481 514 496 510 YKTYGWKLHLYSHPI 775 *1101 4 13 481 514 497 511 KTYGWKLHLYSHPIV 776 *0101 30 13 481 514 497 511 KTYGWKLHLYSHPIV 776 *0701 13 13 481 514 497 511 KTYGWKLHLYSHPIV 776 *1101 3 13 481 514 497 511 KTYGWKLHLYSHPIV 776 *1501 90 13 481 514 498 512 TYGWKLHLYSHPIVL 777 *0101 70 13 481 514 498 512 TYGWKLHLYSHPIVL 777 *0701 71 13 481 514 498 512 TYGWKLHLYSHPIVL 777 *1101 1 13 481 514 498 512 TYGWKLHLYSHPIVL 777 *1501 89 13 481 514 499 513 YGWKLHLYSHPIVLG 778 *0101 81 13 481 514 499 513 YGWKLHLYSHPIVLG 778 *0701 24 13 481 514 499 513 YGWKLHLYSHPIVLG 778 *1301 50 13 481 514 499 513 YGWKLHLYSHPIVLG 778 *1501 87 13 481 514 500 514 GWKLHLYSHPIVLGF 779 *0101 66 13 481 514 500 514 GWKLHLYSHPIVLGF 779 *0701 7 13 481 514 500 514 GWKLHLYSHPIVLGF 779 *1301 49 13 481 514 500 514 GWKLHLYSHPIVLGF 779 *1501 86 13 481 514 Cumulative Class II-B score: 3046 524 538 SPFLLAQFTSAICSV 780 *0101 61 14 524 559 524 538 SPFLLAQFTSAICSV 780 *0401 43 14 524 559 524 538 SPFLLAQFTSAICSV 780 *1501 16 14 524 559 525 539 PFLLAQFTSAICSVV 781 *0101 24 14 524 559 525 539 PFLLAQFTSAICSVV 781 *0401 41 14 524 559 525 539 PFLLAQFTSAICSVV 781 *0701 59 14 524 559 525 539 PFLLAQFTSAICSVV 781 *1501 14 14 524 559 526 540 FLLAQFTSAICSVVR 782 *0401 13 14 524 559 526 540 FLLAQFTSAICSVVR 782 *0701 53 14 524 559 527 541 LLAQFTSAICSVVRR 783 *0701 49 14 524 559 528 542 LAQFTSAICSVVRRA 784 *0701 43 14 524 559 529 543 AQFTSAICSVVRRAF 785 *0701 51 14 524 559 533 547 SAICSVVRRAFPHCL 786 *0701 47 14 524 559 533 547 SAICSVVRRAFPHCL 786 *1301 60 14 524 559 534 548 AICSVVRRAFPHCLA 787 *0701 16 14 524 559 534 548 AICSVVRRAFPHCLA 787 *1301 59 14 524 559 535 549 ICSVVRRAFPHCLAF 788 *0106 10 14 524 559 535 549 ICSVVRRAFPHCLAF 788 *0701 21 14 524 559 535 549 ICSVVRRAFPHCLAF 788 *1301 57 14 524 559 536 550 CSVVRRAFPHCLAFS 789 *0103 30 14 524 559 536 550 CSVVRRAFPHCLAFS 789 *0106 30 14 524 559 536 550 CSVVRRAFPHCLAFS 789 *1301 56 14 524 559 537 551 SVVRRAFPHCLAFSY 790 *1301 54 14 524 559 538 552 VVRRAFPHCLAFSYM 791 *1301 53 14 524 559 539 553 VRRAFPHCLAFSYMD 792 *1301 51 14 524 559 545 559 HCLAFSYMDDVVLGA 793 *0401 30 14 524 559 Cumulative Class II-B score: 1042 526 540 FLLAQFTSAICSVVR 782 *0401 13 15 526 559 526 540 FLLAQFTSAICSVVR 782 *0701 53 15 526 559 527 541 LLAQFTSAICSVVRR 783 *0701 49 15 526 559 528 542 LAQFTSAICSVVRRA 784 *0701 43 15 526 559 529 543 AQFTSAICSVVRRAF 785 *0701 51 15 526 559 533 547 SAICSVVRRAFPHCL 786 *0701 47 15 526 559 533 547 SAICSVVRRAFPHCL 786 *1301 60 15 526 559 534 548 AICSVVRRAFPHCLA 787 *0701 16 15 526 559 534 548 AICSVVRRAFPHCLA 787 *1301 59 15 526 559 535 549 ICSVVRRAFPHCLAF 788 *0106 10 15 526 559 535 549 ICSVVRRAFPHCLAF 788 *0701 21 15 526 559 535 549 ICSVVRRAFPHCLAF 788 *1301 57 15 526 559 536 550 CSVVRRAFPHCLAFS 789 *0103 30 15 526 559 536 550 CSVVRRAFPHCLAFS 789 *0106 30 15 526 559 536 550 CSVVRRAFPHCLAFS 789 *1301 56 15 526 559 537 551 SVVRRAFPHCLAFSY 790 *1301 54 15 526 559 538 552 VVRRAFPHCLAFSYM 791 *1301 53 15 526 559 539 553 VRRAFPHCLAFSYMD 792 *1301 51 15 526 559 545 559 HCLAFSYMDDVVLGA 793 *0401 30 15 526 559 Cumulative Class II-B score: 783 565 579 RESLYTAVTNFLLSL 794 *0103 9 16 565 598 565 579 RESLYTAVTNFLLSL 794 *0701 67 16 565 598 566 580 ESLYTAVTNFLLSLG 795 *0701 66 16 565 598 567 581 SLYTAVTNFLLSLGI 796 *0701 64 16 565 598 568 582 LYTAVTNFLLSLGIH 797 *0701 63 16 565 598 569 583 YTAVTNFLLSLGIHL 798 *0101 90 16 565 598 569 583 YTAVTNFLLSLGIHL 798 *0701 61 16 565 598 569 583 YTAVTNFLLSLGIHL 798 *1501 37 16 565 598 570 584 TAVTNFLLSLGIHLN 799 *0101 91 16 565 598 570 584 TAVTNFLLSLGIHLN 799 *0102 28 16 565 598 570 584 TAVTNFLLSLGIHLN 799 *0104 23 16 565 598 570 584 TAVTNFLLSLGIHLN 799 *1501 49 16 565 598 571 585 AVTNFLLSLGIHLNP 800 *0101 89 16 565 598 571 585 AVTNFLLSLGIHLNP 800 *0102 35 16 565 598 571 585 AVTNFLLSLGIHLNP 800 *0104 25 16 565 598 571 585 AVTNFLLSLGIHLNP 800 *1501 46 16 565 598 572 586 VTNFLLSLGIHLNPN 801 *0101 84 16 565 598 572 586 VTNFLLSLGIHLNPN 801 *0102 38 16 565 598 572 586 VTNFLLSLGIHLNPN 801 *0104 38 16 565 598 572 586 VTNFLLSLGIHLNPN 801 *0106 5 16 565 598 572 586 VTNFLLSLGIHLNPN 801 *1501 63 16 565 598 573 587 TNFLLSLGIHLNPNK 802 *0101 83 16 565 598 573 587 TNFLLSLGIHLNPNK 802 *0102 10 16 565 598 573 587 TNFLLSLGIHLNPNK 802 *0104 5 16 565 598 573 587 TNFLLSLGIHLNPNK 802 *0401 4 16 565 598 573 587 TNFLLSLGIHLNPNK 802 *1501 43 16 565 598 574 588 NFLLSLGIHLNPNKT 803 *0101 33 16 565 598 574 588 NFLLSLGIHLNPNKT 803 *1501 30 16 565 598 575 589 FLLSLGIHLNPNKTK 804 *0101 23 16 565 598 575 589 FLLSLGIHLNPNKTK 804 *1501 29 16 565 598 576 590 LLSLGIHLNPNKTKR 805 *1301 25 16 565 598 577 591 LSLGIHLNPNKTKRW 806 *1301 50 16 565 598 578 592 SLGIHLNPNKTKRWG 807 *1301 43 16 565 598 579 593 LGIHLNPNKTKRWGY 808 *1301 36 16 565 598 Cumulative Class II-B score: 1482 589 603 KRWGYSLNFMGYIIG 809 *1501 57 17 584 617 590 604 RWGYSLNFMGYIIGS 810 *1501 56 17 584 617 591 605 WGYSLNFMGYIIGSW 811 *1501 34 17 584 617 592 606 GYSLNFMGYIIGSWG 812 *1501 21 17 584 617 593 607 YSLNFMGYIIGSWGT 813 *1501 24 17 584 617 594 608 SLNFMGYIIGSWGTL 814 *1501 11 17 584 617 595 609 LNFMGYIIGSWGTLP 815 *1501 19 17 584 617 Cumulative Class II-B score: 223 653 667 YPALMPLYACIQAKQ 816 *1101 11 18 653 691 656 670 LMPLYACIQAKQAFT 817 *0101 58 18 653 691 656 670 LMPLYACIQAKQAFT 817 *0105 58 18 653 691 656 670 LMPLYACIQAKQAFT 817 *0107 58 18 653 691 657 671 MPLYACIQAKQAFTF 818 *0101 75 18 653 691 657 671 MPLYACIQAKQAFTF 818 *0105 75 18 653 691 657 671 MPLYACIQAKQAFTF 818 *0107 75 18 653 691 657 671 MPLYACIQAKQAFTF 818 *1301 41 18 653 691 658 672 PLYACIQAKQAFTFS 819 *0101 48 18 653 691 658 672 PLYACIQAKQAFTFS 819 *0105 48 18 653 691 658 672 PLYACIQAKQAFTFS 819 *0107 48 18 653 691 658 672 PLYACIQAKQAFTFS 819 *1301 40 18 653 691 659 673 LYACIQAKQAFTFSP 820 *1301 39 18 653 691 660 674 YACIQAKQAFTFSPT 821 *1301 37 18 653 691 661 675 ACIQAKQAFTFSPTY 822 *1301 36 18 653 691 662 676 CIQAKQAFTFSPTYK 823 *1301 34 18 653 691 663 677 IQAKQAFTFSPTYKA 824 *0701 6 18 653 691 663 677 IQAKQAFTFSPTYKA 824 *1301 33 18 653 691 664 678 QAKQAFTFSPTYKAF 825 *0401 44 18 653 691 664 678 QAKQAFTFSPTYKAF 825 *0701 37 18 653 691 665 679 AKQAFTFSPTYKAFL 826 *0401 79 18 653 691 665 679 AKQAFTFSPTYKAFL 826 *0701 77 18 653 691 666 680 KQAFTFSPTYKAFLS 827 *0401 33 18 653 691 666 680 KQAFTFSPTYKAFLS 827 *0701 60 18 653 691 666 680 KQAFTFSPTYKAFLS 827 *1101 13 18 653 691 666 680 KQAFTFSPTYKAFLS 827 *1501 8 18 653 691 667 681 QAFTFSPTYKAFLSK 828 *0401 54 18 653 691 667 681 QAFTFSPTYKAFLSK 828 *0701 46 18 653 691 668 682 AFTFSPTYKAFLSKQ 829 *0701 14 18 653 691 669 683 FTFSPTYKAFLSKQY 830 *0701 19 18 653 691 672 686 SPTYKAFLSKQYMNL 831 *1501 3 18 653 691 673 687 PTYKAFLSKQYMNLY 832 *1501 23 18 653 691 677 691 AFLSKQYMNLYPVAR 833 *0101 40 18 653 691 Cumulative Class II-B score: 1365 657 671 MPLYACIQAKQAFTF 818 *0101 75 19 657 691 657 671 MPLYACIQAKQAFTF 818 *0105 75 19 657 691 657 671 MPLYACIQAKQAFTF 818 *0107 75 19 657 691 657 671 MPLYACIQAKQAFTF 818 *1301 41 19 657 691 658 672 PLYACIQAKQAFTFS 819 *0101 48 19 657 691 658 672 PLYACIQAKQAFTFS 819 *0105 48 19 657 691 658 672 PLYACIQAKQAFTFS 819 *0107 48 19 657 691 658 672 PLYACIQAKQAFTFS 819 *1301 40 19 657 691 659 673 LYACIQAKQAFTFSP 820 *1301 39 19 657 691 660 674 YACIQAKQAFTFSPT 821 *1301 37 19 657 691 661 675 ACIQAKQAFTFSPTY 822 *1301 36 19 657 691 662 676 CIQAKQAFTFSPTYK 823 *1301 34 19 657 691 663 677 IQAKQAFTFSPTYKA 824 *0701 6 19 657 691 663 677 IQAKQAFTFSPTYKA 824 *1301 33 19 657 691 664 678 QAKQAFTFSPTYKAF 825 *0401 44 19 657 691 664 678 QAKQAFTFSPTYKAF 825 *0701 37 19 657 691 665 679 AKQAFTFSPTYKAFL 826 *0401 79 19 657 691 665 679 AKQAFTFSPTYKAFL 826 *0701 77 19 657 691 666 680 KQAFTFSPTYKAFLS 827 *0401 33 19 657 691 666 680 KQAFTFSPTYKAFLS 827 *0701 60 19 657 691 666 680 KQAFTFSPTYKAFLS 827 *1101 13 19 657 691 666 680 KQAFTFSPTYKAFLS 827 *1501 8 19 657 691 667 681 QAFTFSPTYKAFLSK 828 *0401 54 19 657 691 667 681 QAFTFSPTYKAFLSK 828 *0701 46 19 657 691 668 682 AFTFSPTYKAFLSKQ 829 *0701 14 19 657 691 669 683 FTFSPTYKAFLSKQY 830 *0701 19 19 657 691 672 686 SPTYKAFLSKQYMNL 831 *1501 3 19 657 691 673 687 PTYKAFLSKQYMNLY 832 *1501 23 19 657 691 677 691 AFLSKQYMNLYPVAR 833 *0101 40 19 657 691 Cumulative Class II-B score: 1181 717 731 MRGTFVAPLPIHTAE 834 *0101 10 20 715 746 717 731 MRGTFVAPLPIHTAE 834 *0105 10 20 715 746 717 731 MRGTFVAPLPIHTAE 834 *0107 10 20 715 746 718 732 RGTFVAPLPIHTAEL 835 *0101 4 20 715 746 718 732 RGTFVAPLPIHTAEL 835 *0102 20 20 715 746 718 732 RGTFVAPLPIHTAEL 835 *0104 30 20 715 746 718 732 RGTFVAPLPIHTAEL 835 *0105 60 20 715 746 718 732 RGTFVAPLPIHTAEL 835 *0106 33 20 715 746 718 732 RGTFVAPLPIHTAEL 835 *0107 60 20 715 746 719 733 GTFVAPLPIHTAELL 836 *0101 6 20 715 746 732 746 LLAACFARSRSGAKL 837 *0701 1 20 715 746 Cumulative Class II-B score: 244 767 781 GCTANWILRGTSFVY 838 *1501 1 21 754 791 768 782 CTANWILRGTSFVYV 839 *1301 21 21 754 791 768 782 CTANWILRGTSFVYV 839 *1501 10 21 754 791 773 787 ILRGTSFVYVPSALN 840 *0101 100 21 754 791 773 787 ILRGTSFVYVPSALN 840 *0401 23 21 754 791 773 787 ILRGTSFVYVPSALN 840 *0701 31 21 754 791 774 788 LRGTSFVYVPSALNP 841 *0101 96 21 754 791 774 788 LRGTSFVYVPSALNP 841 *0105 40 21 754 791 774 788 LRGTSFVYVPSALNP 841 *0107 40 21 754 791 774 788 LRGTSFVYVPSALNP 841 *0401 56 21 754 791 774 788 LRGTSFVYVPSALNP 841 *0701 23 21 754 791 775 789 RGTSFVYVPSALNPA 842 *0101 99 21 754 791 775 789 RGTSFVYVPSALNPA 842 *0102 30 21 754 791 775 789 RGTSFVYVPSALNPA 842 *0104 43 21 754 791 775 789 RGTSFVYVPSALNPA 842 *0105 93 21 754 791 775 789 RGTSFVYVPSALNPA 842 *0107 93 21 754 791 775 789 RGTSFVYVPSALNPA 842 *0401 76 21 754 791 775 789 RGTSFVYVPSALNPA 842 *0701 29 21 754 791 776 790 GTSFVYVPSALNPAD 843 *0101 97 21 754 791 776 790 GTSFVYVPSALNPAD 843 *0102 13 21 754 791 776 790 GTSFVYVPSALNPAD 843 *0104 28 21 754 791 776 790 GTSFVYVPSALNPAD 843 *0105 85 21 754 791 776 790 GTSFVYVPSALNPAD 843 *0107 85 21 754 791 776 790 GTSFVYVPSALNPAD 843 *0401 74 21 754 791 776 790 GTSFVYVPSALNPAD 843 *0701 4 21 754 791 777 791 TSFVYVPSALNPADD 844 *0101 94 21 754 791 777 791 TSFVYVPSALNPADD 844 *0105 68 21 754 791 777 791 TSFVYVPSALNPADD 844 *0107 68 21 754 791 777 791 TSFVYVPSALNPADD 844 *0401 73 21 754 791 Cumulative Class II-B score: 1591 767 781 GCTANWILRGTSFVY 838 *1501 1 22 757 792 768 782 CTANWILRGTSFVYV 839 *1301 21 22 757 792 768 782 CTANWILRGTSFVYV 839 *1501 10 22 757 792 773 787 ILRGTSFVYVPSALN 840 *0101 100 22 757 792 773 787 ILRGTSFVYVPSALN 840 *0401 23 22 757 792 773 787 ILRGTSFVYVPSALN 840 *0701 31 22 757 792 774 788 LRGTSFVYVPSALNP 841 *0101 96 22 757 792 774 788 LRGTSFVYVPSALNP 841 *0105 40 22 757 792 774 788 LRGTSFVYVPSALNP 841 *0107 40 22 757 792 774 788 LRGTSFVYVPSALNP 841 *0401 56 22 757 792 774 788 LRGTSFVYVPSALNP 841 *0701 23 22 757 792 775 789 RGTSFVYVPSALNPA 842 *0101 99 22 757 792 775 789 RGTSFVYVPSALNPA 842 *0102 30 22 757 792 775 789 RGTSFVYVPSALNPA 842 *0104 43 22 757 792 775 789 RGTSFVYVPSALNPA 842 *0105 93 22 757 792 775 789 RGTSFVYVPSALNPA 842 *0107 93 22 757 792 775 789 RGTSFVYVPSALNPA 842 *0401 76 22 757 792 775 789 RGTSFVYVPSALNPA 842 *0701 29 22 757 792 776 790 GTSFVYVPSALNPAD 843 *0101 97 22 757 792 776 790 GTSFVYVPSALNPAD 843 *0102 13 22 757 792 776 790 GTSFVYVPSALNPAD 843 *0104 28 22 757 792 776 790 GTSFVYVPSALNPAD 843 *0105 85 22 757 792 776 790 GTSFVYVPSALNPAD 843 *0107 85 22 757 792 776 790 GTSFVYVPSALNPAD 843 *0401 74 22 757 792 776 790 GTSFVYVPSALNPAD 843 *0701 4 22 757 792 777 791 TSFVYVPSALNPADD 844 *0101 94 22 757 792 777 791 TSFVYVPSALNPADD 844 *0105 68 22 757 792 777 791 TSFVYVPSALNPADD 844 *0107 68 22 757 792 777 791 TSFVYVPSALNPADD 844 *0401 73 22 757 792 778 792 SFVYVPSALNPADDP 845 *0101 54 22 757 792 778 792 SFVYVPSALNPADDP 845 *0401 64 22 757 792 Cumulative Class II-B score: 1709 767 781 GCTANWILRGTSFVY 838 *1501 1 23 754 789 768 782 CTANWILRGTSFVYV 839 *1301 21 23 754 789 768 782 CTANWILRGTSFVYV 839 *1501 10 23 754 789 773 787 ILRGTSFVYVPSALN 840 *0101 100 23 754 789 773 787 ILRGTSFVYVPSALN 840 *0401 23 23 754 789 773 787 ILRGTSFVYVPSALN 840 *0701 31 23 754 789 774 788 LRGTSFVYVPSALNP 841 *0101 96 23 754 789 774 788 LRGTSFVYVPSALNP 841 *0105 40 23 754 789 774 788 LRGTSFVYVPSALNP 841 *0107 40 23 754 789 774 788 LRGTSFVYVPSALNP 841 *0401 56 23 754 789 774 788 LRGTSFVYVPSALNP 841 *0701 23 23 754 789 775 789 RGTSFVYVPSALNPA 842 *0101 99 23 754 789 775 789 RGTSFVYVPSALNPA 842 *0102 30 23 754 789 775 789 RGTSFVYVPSALNPA 842 *0104 43 23 754 789 775 789 RGTSFVYVPSALNPA 842 *0105 93 23 754 789 775 789 RGTSFVYVPSALNPA 842 *0107 93 23 754 789 775 789 RGTSFVYVPSALNPA 842 *0401 76 23 754 789 775 789 RGTSFVYVPSALNPA 842 *0701 29 23 754 789 Cumulative Class II-B score: 903 “Start” and “End” are relative to the amino acid sequence of human HBV polymerase as depicted in SEQ ID NO: 1 ^(A) Peptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV polymerase is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)Class II-B score. See Material and Methods (Examples section). ^(C)Cumulative Class II-B score. See Material and Methods (Examples section).

TABLE 5a Predicted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences from HBV Core protein. HLA class I binding peptides in SLP sequences derived from HBV Peptide of invention Core protein (SLP) SEQ ID HLA class Class I-B Class I-BCI Start End Length Sequence ^(A) NO: I molecule score^(B) C-score^(C) score^(D) SLP# SLP Start SLP End 107 117 11 DPASRDLVVNY 846 B*3501 100 1.68 168 24 107 141 107 117 11 DPASRDLVVNY 846 B*3503 30 1.68 50 24 107 141 107 117 11 DPASRDLVVNY 846 B*5301 79 1.68 132 24 107 141 108 117 10 PASRDLVVNY 847 B*5701 100 1.68 168 24 107 141 108 117 10 PASRDLVVNY 847 B*5801 100 1.68 168 24 107 141 109 117 9 ASRDLVVNY 848 A*3002 45 1.68 76 24 107 141 109 117 9 ASRDLVVNY 848 B*1501 40 1.68 67 24 107 141 109 117 9 ASRDLVVNY 848 B*1525 10 1.68 17 24 107 141 111 118 8 RDLVVNYV 849 B*1302 63 1.72 108 24 107 141 113 122 10 LVVNYVNTNV 850 A*0206 29 1.04 30 24 107 141 113 122 10 LVVNYVNTNV 850 A*6802 75 1.04 78 24 107 141 114 122 9 VVNYVNTNV 851 A*6802 38 1.04 39 24 107 141 113 123 11 LVVNYVNTNVG 852 A*6802 25 0.09 2 24 107 141 116 124 9 NYVNTNVGL 853 A*2301 63 1.89 118 24 107 141 117 125 9 YVNTNVGLK 854 A*0301 100 0.33 33 24 107 141 117 125 9 YVNTNVGLK 854 A*1101 100 0.33 33 24 107 141 117 125 9 YVNTNVGLK 854 A*6801 62 0.33 20 24 107 141 116 126 11 NYVNTNVGLKI 855 A*2301 44 1.53 67 24 107 141 116 126 11 NYVNTNVGLKI 855 A*2402 63 1.53 96 24 107 141 120 129 10 TNVGlKIRQL 856 B*0801 50 1.67 83 24 107 141 121 129 9 NVGLKIRQL 857 B*0702 75 1.67 125 24 107 141 121 130 10 NVGLKIRQLL 858 B*0702 83 1.23 103 24 107 141 123 130 8 GLKIRQLL 859 B*0801 70 1.23 86 24 107 141 122 131 10 VGLKIRQLLW 860 B*5802 55 1.66 91 24 107 141 123 132 10 GLKIRQLLWF 861 A*0301 25 1.02 25 24 107 141 125 132 8 KIRQLLWF 862 A*3201 75 1.02 76 24 107 141 125 132 8 KIRQLLWF 862 B*1501 20 1.02 20 24 107 141 125 132 8 KIRQLLWF 862 B*1525 40 1.02 41 24 107 141 126 134 9 IRQLLWFHI 863 B*2702 86 1.69 145 24 107 141 126 134 9 IRQLLWFHI 863 B*2705 84 1.69 142 24 107 141 127 134 8 RQLLWFHI 864 A*2301 81 1.69 138 24 107 141 127 134 8 RQLLWFHI 864 A*2402 69 1.69 116 24 107 141 127 134 8 RQLLWFHI 864 A*3201 63 1.69 106 24 107 141 127 134 8 RQLLWFHI 864 B*1301 90 1.69 152 24 107 141 127 134 8 RQLLWFHI 864 B*2702 100 1.69 169 24 107 141 127 134 8 RQLLWFHI 864 B*3701 73 1.69 124 24 107 141 127 134 8 RQLLWFHI 864 B*4002 57 1.69 97 24 107 141 127 134 8 RQLLWFHI 864 B*4801 100 1.69 169 24 107 141 127 134 8 RQLLWFHI 864 B*4901 47 1.69 80 24 107 141 127 134 8 RQLLWFHI 864 B*5001 47 1.69 79 24 107 141 127 134 8 RQLLWFHI 864 B*5201 78 1.69 132 24 107 141 126 135 10 IRQLLWFHIS 865 B*2705 3 0.55 2 24 107 141 127 135 9 RQLLWFHIS 866 B*4801 14 0.55 8 24 107 141 127 136 10 RQLLWFHISC 867 B*4801 29 0.82 24 24 107 141 128 136 9 QLLWFHISC 868 A*0201 75 0.82 62 24 107 141 129 136 8 LLWFHISC 869 A*0201 60 0.82 49 24 107 141 127 137 11 RQLLWFHISCL 870 B*1301 35 1.95 68 24 107 141 127 137 11 RQLLWFHISCL 870 B*1302 50 1.95 98 24 107 141 127 137 11 RQLLWFHISCL 870 B*1402 38 1.95 75 24 107 141 127 137 11 RQLLWFHISCL 870 B*2702 71 1.95 139 24 107 141 127 137 11 RQLLWFHISCL 870 B*3701 40 1.95 78 24 107 141 127 137 11 RQLLWFHISCL 870 B*3901 64 1.95 125 24 107 141 127 137 11 RQLLWFHISCL 870 B*4001 7 1.95 13 24 107 141 127 137 11 RQLLWFHISCL 870 B*4002 14 1.95 28 24 107 141 128 137 10 QLLWFHISCL 871 A*0201 20 1.95 39 24 107 141 129 137 9 LLWFHISCL 872 A*0201 50 1.95 98 24 107 141 129 137 9 LLWFHISCL 872 B*0801 50 1.95 98 24 107 141 130 137 8 LWFHISCL 873 A*2301 13 1.95 24 24 107 141 130 137 8 LWFHISCL 873 A*2402 13 1.95 24 24 107 141 129 138 10 LLWFHISCLT 874 A*0201 56 0.32 18 24 107 141 129 139 11 LLWFHISCLTF 875 A*3201 81 1.49 121 24 107 141 129 139 11 LLWFHISCLTF 875 B*1501 100 1.49 149 24 107 141 129 139 11 LLWFHISCLTF 875 B*1502 78 1.49 116 24 107 141 129 139 11 LLWFHISCLTF 875 B*1525 100 1.49 149 24 107 141 130 139 10 LWFHISCLTF 876 A*2301 100 1.49 149 24 107 141 130 139 10 LWFHISCLTF 876 A*2402 100 1.49 149 24 107 141 130 139 10 LWFHISCLTF 876 A*2902 86 1.49 127 24 107 141 130 139 10 LWFHISCLTF 876 B*2702 43 1.49 64 24 107 141 132 139 8 FHISCLTF 877 A*2301 56 1.49 84 24 107 141 132 139 8 FHISCLTF 877 B*1402 54 1.49 80 24 107 141 132 139 8 FHISCLTF 877 B*3503 40 1.49 59 24 107 141 132 139 8 FHISCLTF 877 B*3801 100 1.49 149 24 107 141 132 139 8 FHISCLTF 877 B*3901 57 1.49 85 24 107 141 131 141 11 WFHISCLTFGR 878 A*3101 29 1.41 42 24 107 141 131 141 11 WFHISCLTFGR 878 A*3303 52 1.41 74 24 107 141 132 141 10 FHISCLTFGR 879 A*3101 35 1.41 50 24 107 141 133 141 9 HISCLTFGR 880 A*3101 82 1.41 116 24 107 141 133 141 9 HISCLTFGR 880 A*3303 95 1.41 135 24 107 141 133 141 9 HISCLTFGR 880 A*6801 85 1.41 120 24 107 141 133 141 9 HISCLTFGR 880 A*7401 100 1.41 141 24 107 141 134 141 8 ISCLTFGR 881 A*3101 88 1.41 125 24 107 141 134 141 8 ISCLTFGR 881 A*3303 29 1.41 40 24 107 141 134 141 8 ISCLTFGR 881 A*6801 31 1.41 43 24 107 141 134 141 8 ISCLTFGR 881 A*7401 50 1.41 71 24 107 141 Cumulative Class I-BCI score^(E): 7277 136 145 10 CLTFGRETVL 882 B*0801 100 1.87 187 25 136 169 137 147 11 LTFGRETVLEY 883 A*0101 80 1.68 134 25 136 169 137 147 11 LTFGRETVLEY 883 A*0301 67 1.68 112 25 136 169 137 147 11 LTFGRETVLEY 883 A*2501 80 1.68 134 25 136 169 137 147 11 LTFGRETVLEY 883 A*2601 60 1.68 101 25 136 169 137 147 11 LTFGRETVLEY 883 A*2902 100 1.68 168 25 136 169 137 147 11 LTFGRETVLEY 883 A*3002 100 1.68 168 25 136 169 137 147 11 LTFGRETVLEY 883 B*1501 90 1.68 151 25 136 169 137 147 11 LTFGRETVLEY 883 B*1502 100 1.68 168 25 136 169 137 147 11 LTFGRETVLEY 883 B*4601 67 1.68 112 25 136 169 137 147 11 LTFGRETVLEY 883 B*5701 38 1.68 63 25 136 169 137 147 11 LTFGRETVLEY 883 B*5802 36 1.68 61 25 136 169 139 147 9 FGRETVLEY 884 B*1525 90 1.68 151 25 136 169 139 147 9 FGRETVLEY 884 B*4601 100 1.68 168 25 136 169 138 148 11 TFGRETVLEYL 885 A*2301 6 1.23 8 25 136 169 138 148 11 TFGRETVLEYL 885 A*2402 31 1.23 38 25 136 169 139 148 10 FGRETVLEYL 886 B*0702 100 1.23 123 25 136 169 140 148 9 GRETVLEYL 887 B*2702 21 1.23 26 25 136 169 141 148 8 RETVLEYL 888 B*1301 60 1.23 74 25 136 169 141 148 8 RETVLEYL 888 B*3701 33 1.23 41 25 136 169 141 148 8 RETVLEYL 888 B*4001 100 1.23 123 25 136 169 141 148 8 RETVLEYL 888 B*4002 93 1.23 114 25 136 169 141 148 8 RETVLEYL 888 B*4402 8 1.23 10 25 136 169 141 148 8 RETVLEYL 888 B*4403 54 1.23 66 25 136 169 141 148 8 RETVLEYL 888 B*4801 7 1.23 9 25 136 169 141 148 8 RETVLEYL 888 B*4901 6 1.23 7 25 136 169 139 149 11 FGRETVLEYLV 889 A*0201 45 1.23 55 25 136 169 141 149 9 RETVLEYLV 890 B*1301 30 1.23 37 25 136 169 141 149 9 RETVLEYLV 890 B*1302 38 1.23 46 25 136 169 141 149 9 RETVLEYLV 890 B*3701 27 1.23 33 25 136 169 141 149 9 RETVLEYLV 890 B*4001 67 1.23 82 25 136 169 141 149 9 RETVLEYLV 890 B*4002 79 1.23 96 25 136 169 141 149 9 RETVLEYLV 890 B*4901 71 1.23 87 25 136 169 141 149 9 RETVLEYLV 890 B*5001 27 1.23 33 25 136 169 142 149 8 ETVLEYLV 891 A*2501 20 1.23 25 25 136 169 142 149 8 ETVLEYLV 891 A*2601 50 1.23 61 25 136 169 141 150 10 RETVLEYLVS 892 B*4002 7 0.57 4 25 136 169 141 151 11 RETVLEYLVSF 893 B*1301 45 1.50 67 25 136 169 141 151 11 RETVLEYLVSF 893 B*1801 88 1.50 131 25 136 169 141 151 11 RETVLEYLVSF 893 B*2702 50 1.50 75 25 136 169 141 151 11 RETVLEYLVSF 893 B*4001 80 1.50 120 25 136 169 141 151 11 RETVLEYLVSF 893 B*4002 86 1.50 128 25 136 169 141 151 11 RETVLEYLVSF 893 B*4402 67 1.50 100 25 136 169 141 151 11 RETVLEYLVSF 893 B*4403 77 1.50 115 25 136 169 141 151 11 RETVLEYLVSF 893 B*4901 35 1.50 53 25 136 169 141 151 11 RETVLEYLVSF 893 B*5001 60 1.50 90 25 136 169 142 151 10 ETVLEYLVSF 894 A*2501 100 1.50 150 25 136 169 142 151 10 ETVLEYLVSF 894 A*2601 100 1.50 150 25 136 169 143 151 9 TVLEYLVSF 895 A*3201 50 1.50 75 25 136 169 143 151 9 TVLEYLVSF 895 B*1525 20 1.50 30 25 136 169 145 152 8 LEYLVSFG 896 B*4901 18 0.48 8 25 136 169 143 153 11 TVLEYLVSFGV 897 A*0201 90 1.80 162 25 136 169 143 153 11 TVLEYLVSFGV 897 A*6802 100 1.80 180 25 136 169 144 153 10 VLEYLVSFGV 898 A*0201 65 1.80 117 25 136 169 145 153 9 LEYLVSFGV 899 A*0201 67 1.80 120 25 136 169 145 153 9 LEYLVSFGV 899 B*1301 75 1.80 135 25 136 169 145 153 9 LEYLVSFGV 899 B*1801 63 1.80 113 25 136 169 145 153 9 LEYLVSFGV 899 B*3701 67 1.80 120 25 136 169 145 153 9 LEYLVSFGV 899 B*4001 73 1.80 132 25 136 169 145 153 9 LEYLVSFGV 899 B*4002 29 1.80 51 25 136 169 145 153 9 LEYLVSFGV 899 B*4402 42 1.80 75 25 136 169 145 153 9 LEYLVSFGV 899 B*4901 94 1.80 170 25 136 169 145 153 9 LEYLVSFGV 899 B*5001 87 1.80 156 25 136 169 145 153 9 LEYLVSFGV 899 B*5201 56 1.80 100 25 136 169 145 154 10 LEYLVSFGVW 900 B*1301 65 1.34 87 25 136 169 145 154 10 LEYLVSFGVW 900 B*1302 13 1.34 17 25 136 169 145 154 10 LEYLVSFGVW 900 B*3801 11 1.34 15 25 136 169 145 154 10 LEYLVSFGVW 900 B*4402 92 1.34 123 25 136 169 145 154 10 LEYLVSFGVW 900 B*4403 92 1.34 124 25 136 169 145 154 10 LEYLVSFGVW 900 B*4901 88 1.34 118 25 136 169 145 154 10 LEYLVSFGVW 900 B*5201 22 1.34 30 25 136 169 146 154 9 EYLVSFGVW 901 A*2301 69 1.34 92 25 136 169 146 154 9 EYLVSFGVW 901 A*2402 81 1.34 109 25 136 169 147 154 8 YLVSFGVW 902 B*5701 13 1.34 17 25 136 169 147 154 8 YLVSFGVW 902 B*5801 36 1.34 48 25 136 169 145 155 11 LEYLVSFGVWI 903 B*1301 85 1.63 139 25 136 169 145 155 11 LEYLVSFGVWI 903 B*1302 88 1.63 143 25 136 169 145 155 11 LEYLVSFGVWI 903 B*1801 50 1.63 82 25 136 169 145 155 11 LEYLVSFGVWI 903 B*3701 80 1.63 130 25 136 169 145 155 11 LEYLVSFGVWI 903 B*3801 78 1.63 127 25 136 169 145 155 11 LEYLVSFGVWI 903 B*4001 60 1.63 98 25 136 169 145 155 11 LEYLVSFGVWI 903 B*4002 43 1.63 70 25 136 169 145 155 11 LEYLVSFGVWI 903 B*4402 50 1.63 82 25 136 169 145 155 11 LEYLVSFGVWI 903 B*4403 62 1.63 100 25 136 169 145 155 11 LEYLVSFGVWI 903 B*4901 100 1.63 163 25 136 169 145 155 11 LEYLVSFGVWI 903 B*5001 80 1.63 130 25 136 169 145 155 11 LEYLVSFGVWI 903 B*5201 89 1.63 145 25 136 169 147 155 9 YLVSFGVWI 904 A*0201 75 1.63 122 25 136 169 146 156 11 EYLVSFGVWIR 905 A*3303 71 1.61 115 25 136 169 147 156 10 YLVSFGVWIR 906 A*0301 100 1.61 161 25 136 169 147 156 10 YLVSFGVWIR 906 A*6801 54 1.61 87 25 136 169 148 156 9 LVSFGVWIR 907 A*3101 12 1.61 19 25 136 169 148 156 9 LVSFGVWIR 907 A*3303 38 1.61 61 25 136 169 148 156 9 LVSFGVWIR 907 A*6801 23 1.61 37 25 136 169 148 156 9 LVSFGVWIR 907 A*7401 40 1.61 64 25 136 169 149 156 8 VSFGVWIR 908 A*1101 13 1.61 20 25 136 169 149 156 8 VSFGVWIR 908 A*3101 59 1.61 95 25 136 169 149 156 8 VSFGVWIR 908 A*3303 48 1.61 77 25 136 169 149 156 8 VSFGVWIR 908 A*6801 77 1.61 124 25 136 169 149 156 8 VSFGVWIR 908 A*7401 80 1.61 129 25 136 169 148 157 10 LVSFGVWIRT 909 A*3201 88 0.42 37 25 136 169 148 158 11 LVSFGVWIRTP 910 A*6802 63 0.28 17 25 136 169 151 160 10 FGVWIRTPPA 911 B*5501 55 0.99 54 25 136 169 151 160 10 FGVWIRTPPA 911 B*5601 64 0.99 63 25 136 169 151 161 11 FGVWIRTPPAY 912 A*2902 57 1.46 83 25 136 169 151 161 11 FGVWIRTPPAY 912 B*1502 56 1.46 81 25 136 169 151 161 11 FGVWIRTPPAY 912 B*3501 89 1.46 130 25 136 169 151 161 11 FGVWIRTPPAY 912 B*4601 33 1.46 49 25 136 169 152 161 10 GVWIRTPPAY 913 A*3001 67 1.46 97 25 136 169 152 161 10 GVWIRTPPAY 913 B*1502 22 1.46 32 25 136 169 153 161 9 VWIRTPPAY 914 A*2902 79 1.46 114 25 136 169 153 161 9 VWIRTPPAY 914 A*3002 91 1.46 132 25 136 169 154 161 8 WIRTPPAY 915 A*2601 30 1.46 44 25 136 169 154 161 8 WIRTPPAY 915 A*2902 14 1.46 21 25 136 169 154 161 8 WIRTPPAY 915 B*1501 70 1.46 102 25 136 169 154 161 8 WIRTPPAY 915 B*1502 89 1.46 130 25 136 169 154 161 8 WIRTPPAY 915 B*1525 50 1.46 73 25 136 169 152 162 11 GVWIRTPPAYR 916 A*0301 33 0.95 32 25 136 169 152 162 11 GVWIRTPPAYR 916 A*1101 38 0.95 36 25 136 169 152 162 11 GVWIRTPPAYR 916 A*3101 100 0.95 95 25 136 169 152 162 11 GVWIRTPPAYR 916 A*3303 76 0.95 72 25 136 169 152 162 11 GVWIRTPPAYR 916 A*7401 90 0.95 86 25 136 169 153 162 10 VWIRTPPAYR 917 A*3101 6 0.95 6 25 136 169 153 162 10 VWIRTPPAYR 917 A*3303 33 0.95 32 25 136 169 154 162 9 WIRTPPAYR 918 A*3303 90 0.95 86 25 136 169 154 162 9 WIRTPPAYR 918 A*7401 70 0.95 67 25 136 169 156 165 10 RTPPAYRPPN 919 A*3001 83 0.09 7 25 136 169 158 168 11 PPAYRPPNAPI 920 B*0702 17 1.00 17 25 136 169 160 168 9 AYRPPNAPI 921 A*2402 25 1.00 25 25 136 169 160 168 9 AYRPPNAPI 921 A*3001 42 1.00 41 25 136 169 160 169 10 AYRPPNAPIL 922 A*2402 6 1.90 12 25 136 169 160 169 10 AYRPPNAPIL 922 B*0702 50 1.90 95 25 136 169 161 169 9 YRPPNAPIL 923 B*3901 36 1.90 68 25 136 169 Cumulative BCI Class I-score: 11331 “Start” and “End” are relative to the amino acid sequence of HBV core protein as depicted in SEQ ID NO: 4 ^(A) Peptide amino acid sequence. Each HLA class I binding peptide of HBV core protein is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods of Examples section. ^(C)C-score. See Material and Methods of Examples section. ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 5b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV Core protein. HLA class II binding peptides in SLP Peptide of sequences derived from HBV Core protein invention (SLP) SEQ HLA- Class ID DRB1 II-B SLP SLP Start End Sequence^(A) NO: molecule score^(B) SLP# Start End 107 121 DPASRDLVVNYVNTN 924 *0301   46 24 107 141 108 122 PASRDLVVNYVNTNV 925 *0401   69 24 ″ ″ 108 122 PASRDLVVNYVNTNV ″ *1301   10 24 ″ ″ 109 123 ASRDLVVNYVNTNVG 926 *0401   85 24 ″ ″ 109 123 ASRDLVVNYVNTNVG ″ *1301   20 24 ″ ″ 110 124 SRDLVVNYVNTNVGL 927 *0401   92 24 ″ ″ 110 124 SRDLVVNYVNTNVGL ″ *1301   40 24 ″ ″ 111 125 RDLVVNYVNTNVGLK 928 *0103   17 24 ″ ″ 111 125 RDLVVNYVNTNVGLK ″ *0401  100 24 ″ ″ 111 125 RDLVVNYVNTNVGLK ″ *1301   50 24 ″ ″ 112 126 DLVVNYVNTNVGLKI 929 *0103   50 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0106   25 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0301   62 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0401   77 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0701   15 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *1301   80 24 ″ ″ 113 127 LVVNYVNTNVGLKIR 930 *0103  100 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0104   35 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0106   75 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0301   69 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0701   50 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *1301  100 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ 931 *0103   83 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ ″ *0104   45 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ ″ *0106   80 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ ″ *1301   90 24 ″ ″ 115 129 VNYVNTNVGLKIRQL 932 *0101   21 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0102   10 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0103   67 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0104   65 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0105   19 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0106   85 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0107   21 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0701   33 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *1301   70 24 ″ ″ 116 130 NYVNTNVGLKIRQLL 933 *0103   33 24 ″ ″ 116 130 NYVNTNVGLKIRQLL ″ *0104   25 24 ″ ″ 116 130 NYVNTNVGLKIRQLL ″ *0106   65 24 ″ ″ 116 130 NYVNTNVGLKIRQLL ″ *1301   60 24 ″ ″ 117 131 YVNTNVGLKIRQLLW 934 *1101   54 24 ″ ″ 117 131 YVNTNVGLKIRQLLW ″ *1301   30 24 ″ ″ 118 132 VNTNVGLKIRQLLWF 935 *0301   38 24 ″ ″ 118 132 VNTNVGLKIRQLLWF ″ *1301   46 24 ″ ″ 119 133 NTNVGLKIRQLLWFH 936 *0301   31 24 ″ ″ 119 133 NTNVGLKIRQLLWFH ″ *1301   38 24 ″ ″ 120 134 TNVGLKIRQLLWFHI 937 *0102   70 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0104   55 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0106   40 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0301   23 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0701   38 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *1301   31 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *1501   38 24 ″ ″ 121 135 NVGLKIRQLLWFHIS 938 *0101   11 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0102   85 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0104   75 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0105   10 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0106   50 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0107   11 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0301   15 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0701   23 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *1301   23 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *1501   85 24 ″ ″ 122 136 VGLKIRQLLWFHISC 939 *0102   65 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *0104   50 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *0106   20 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *0301    8 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *1301   15 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *1501   46 24 ″ ″ 123 137 GLKIRQLLWFHISCL 940 *0101   31 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0102   75 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0104   80 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0106   55 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0701  100 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *1301    8 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *1501  100 24 ″ ″ 124 138 LKIRQLLWFHISCLT 941 *0101   26 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0102   80 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0104   70 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0105   24 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0106   60 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0107   26 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0701   92 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *1501   92 24 ″ ″ 125 139 KIRQLLWFHISCLTF 942 *0101    5 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0102   50 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0104   40 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0105    5 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0106   35 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0107    5 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0701   85 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *1501   31 24 ″ ″ 126 140 IRQLLWFHISCLTFG 943 *0102   40 24 ″ ″ 126 140 IRQLLWFHISCLTFG ″ *0701   46 24 ″ ″ 126 140 IRQLLWFHISCLTFG ″ *1101   69 24 ″ ″ 127 141 RQLLWFHISCLTFGR 944 *0701    8 24 ″ ″ 127 141 RQLLWFHISCLTFGR ″ *1101   46 24 ″ ″ Cumulative Class II-B score^(C): 4649 139 153 FGRETVLEYLVSFGV 945 *0101   42 25 136 169 139 153 FGRETVLEYLVSFGV ″ *0102   35 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *0105   38 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *0107   42 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *0701   69 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *1501   23 25 ″ ″ 140 154 GRETVLEYLVSFGVW 946 *0101   46 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0102   55 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0104   60 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0105   67 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0106   45 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0107   74 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0701   62 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *1501   15 25 ″ ″ 141 155 RETVLEYLVSFGVWI 947 *0101   92 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0102   95 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0104   90 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0105   81 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0106   90 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0107   89 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0701   77 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *1501    8 25 ″ ″ 142 156 ETVLEYLVSFGVWIR 948 *0101  100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0102  100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0104  100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0105   90 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0106  100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0107  100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0701   54 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *1301  100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *1501   77 25 ″ ″ 143 157 TVLEYLVSFGVWIRT 949 *0101   85 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0102   90 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0104   95 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0105   86 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0106   95 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0107   95 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0701   31 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *1301   92 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *1501   69 25 ″ ″ 144 158 VLEYLVSFGVWIRTP 950 *0101   69 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0102   60 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0104   85 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0105   76 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0106   70 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0107   84 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *1301   85 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *1501   62 25 ″ ″ 145 159 LEYLVSFGVWIRTPP 951 *0101   62 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0102   15 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0104   20 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0105   48 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0107   53 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *1301   77 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *1501   54 25 ″ ″ 146 160 EYLVSFGVWIRTPPA 952 *1301   69 25 ″ ″ 147 161 YLVSFGVWIRTPPAY 953 *1301   62 25 ″ ″ 148 162 LVSFGVWIRTPPAYR 954 *0101   32 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *0105   29 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *0107   32 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *0401   40 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *1301   54 25 ″ ″ 149 163 VSFGVWIRTPPAYRP 955 *0101   63 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0102   25 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0105   57 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0107   63 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0401   60 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *1101   25 25 ″ ″ 150 164 SFGVWIRTPPAYRPP 956 *0101   68 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0102   30 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0105   62 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0107   68 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0401   80 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *1101   75 25 ″ ″ 151 165 FGVWIRTPPAYRPPN 957 *0101   79 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0102   45 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0104   30 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0105   71 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0106    5 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0107   79 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0401  100 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *1101  100 25 ″ ″ 152 166 GVWIRTPPAYRPPNA 958 *0101   58 25 ″ ″ 152 166 GVWIRTPPAYRPPNA ″ *0105   52 25 ″ ″ 152 166 GVWIRTPPAYRPPNA ″ *0107   58 25 ″ ″ 152 166 GVWIRTPPAYRPPNA ″ *1101   50 25 ″ ″ Cumulative Class II-B score: 5493 “Start” and “End” are relative to the amino acid sequence of human HBV core protein as depicted in SEQ ID NO: 4 ^(A)Peptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV core is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)Class II-B score. See Material and Methods (Examples section). ^(C)Cumulative Class II-B score. See Material and Methods (Examples section).

TABLE 6a Predicted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences from HBV X protein (consensus sequence). HLA class I binding peptides in SLP sequences Peptide of derived from HBV X protein (consensus sequence) invention (SLP) SEQ HLA Class Class ID class I I-B I-BCI SLP SLP Start End Length Sequence^(A) NO: molecule score^(B) C-score^(C) score^(D) SLP# Start End  36  44  9 ALPSPSPSA  959 A*0201  20 0,97   19 26  36  68  37  44  8 LPSPSPSA  960 B*3501  92 ″   89 26 ″ ″  37  44  8 LPSPSPSA ″ B*5101  82 ″   79 26 ″ ″  37  44  8 LPSPSPSA ″ B*5501  63 ″   61 26 ″ ″  37  44  8 LPSPSPSA ″ B*5601  92 ″   89 26 ″ ″  36  45 10 ALPSPSPSAV  961 A*0201  90 1,49  134 26 ″ ″  37  45  9 LPSPSPSAV  962 B*3503  75 ″  112 26 ″ ″  37  45  9 LPSPSPSAV ″ B*5101 100 ″  149 26 ″ ″  37  45  9 LPSPSPSAV ″ B*5501  94 ″  139 26 ″ ″  37  45  9 LPSPSPSAV ″ B*5601  46 ″   69 26 ″ ″  37  45  9 LPSPSPSAV ″ B*0701  50 ″   74 26 ″ ″  37  47 11 LPSPSPSAVPA  963 A*6802  20 1,05   21 26 ″ ″  37  47 11 LPSPSPSAVPA ″ B*3501  33 ″   35 26 ″ ″  37  47 11 LPSPSPSAVPA ″ B*3503  58 ″   61 26 ″ ″  37  47 11 LPSPSPSAVPA ″ B*5101  55 ″   57 26 ″ ″  37  47 11 LPSPSPSAVPA ″ B*5501  88 ″   92 26 ″ ″  37  47 11 LPSPSPSAVPA ″ B*5601  77 ″   81 26 ″ ″  37  47 11 LPSPSPSAVPA ″ B*0701  25 ″   26 26 ″ ″  39  47  9 SPSPSAVPA  964 B*5501  56 ″   59 26 ″ ″  39  47  9 SPSPSAVPA ″ B*5601  85 ″   89 26 ″ ″  41  51 11 SPSAVPADHGA  965 B*5501   6 1,30    8 26 ″ ″  41  51 11 SPSAVPADHGA ″ B*5601   8 ″   10 26 ″ ″  44  53 10 AVPADHGAHL  966 B*0701  75 1,87  140 26 ″ ″  45  53  9 VPADHGAHL  967 B*1402  43 ″   80 26 ″ ″  45  53  9 VPADHGAHL ″ B*3503  42 ″   78 26 ″ ″  45  53  9 VPADHGAHL ″ B*5501  31 ″   59 26 ″ ″  45  53  9 VPADHGAHL ″ B*0701 100 ″  187 26 ″ ″  45  55 11 VPADHGAHLSL  968 B*1402  93 1,93  180 26 ″ ″  45  55 11 VPADHGAHLSL ″ B*3501  67 ″  129 26 ″ ″  45  55 11 VPADHGAHLSL ″ B*3503 100 ″  193 26 ″ ″  45  55 11 VPADHGAHLSL ″ B*5101  73 ″  141 26 ″ ″  45  55 11 VPADHGAHLSL ″ B*5301  29 ″   55 26 ″ ″  45  55 11 VPADHGAHLSL ″ B*5501  50 ″   97 26 ″ ″  45  55 11 VPADHGAHLSL ″ B*0701 100 ″  193 26 ″ ″  47  55  9 ADHGAHLSL  969 B*4002  14 ″   28 26 ″ ″  48  55  8 DHGAHLSL  970 B*1402  79 ″  152 26 ″ ″  49  56  8 HGAHLSLR  971 A*3303  73 0,63   46 26 ″ ″  49  56  8 HGAHLSLR ″ A*6801  33 ″   21 26 ″ ″  50  58  9 GAHLSLRGL  972 B*0701  25 1,33   33 26 ″ ″  51  58  8 AHLSLRGL  973 B*1402  29 ″   38 26 ″ ″  51  58  8 AHLSLRGL ″ B*3901   9 ″   12 26 ″ ″  51  60 10 AHLSLRGLPV  974 B*1402  71 1,05   75 26 ″ ″  51  60 10 AHLSLRGLPV ″ B*3901  36 ″   38 26 ″ ″  52  60  9 HLSLRGLPV  975 B*0801  40 ″   42 26 ″ ″  53  60  8 LSLRGLPV  976 A*0201  36 ″   38 26 ″ ″  53  60  8 LSLRGLPV ″ B*5201  33 ″   35 26 ″ ″  52  61 10 HLSLRGLPVC  977 A*3001  88 0,87   77 26 ″ ″  53  61  9 LSLRGLPVC  978 B*5802  10 ″    9 26 ″ ″  53  63 11 LSLRGLPVCAF  979 B*1502  71 1,48  106 26 ″ ″  53  63 11 LSLRGLPVCAF ″ B*1525  85 ″  125 26 ″ ″  53  63 11 LSLRGLPVCAF ″ B*4601  50 ″   74 26 ″ ″  53  63 11 LSLRGLPVCAF ″ B*5701 100 ″  148 26 ″ ″  53  63 11 LSLRGLPVCAF ″ B*5801  90 ″  133 26 ″ ″  53  63 11 LSLRGLPVCAF ″ B*5802  30 ″   44 26 ″ ″  54  63 10 SLRGIPVCAF  980 A*0301 100 ″  148 26 ″ ″  54  63 10 SLRGLPVCAF  981 B*1501  86 ″  127 26 ″ ″  54  63 10 SLRGLPVCAF ″ B*1502  86 ″  127 26 ″ ″  54  63 10 SLRGLPVCAF ″ B*1525  54 ″   80 26 ″ ″  54  63 10 SLRGLPVCAF ″ B*4601  36 ″   53 26 ″ ″  56  63  8 RGLPVCAF  982 A*2301  25 ″   37 26 ″ ″  56  63  8 RGLPVCAF ″ A*3201  20 ″   30 26 ″ ″  58  65  8 LPVCAFSS  983 B*5101  45 0,59   27 26 ″ ″  58  65  8 LPVCAFSS ″ B*5501  13 ″    7 26 ″ ″  58  65  8 LPVCAFSS ″ B*5601  31 ″   18 26 ″ ″  56  66 11 RGLPVCAFSSA  984 A*3001  29 0,95   28 26 ″ ″  57  66 10 GLPVCAFSSA  985 A*0201  20 ″   19 26 ″ ″  58  66  9 LPVCAFSSA  986 B*3503  83 ″   79 26 ″ ″  58  66  9 LPVCAFSSA ″ B*5101  91 ″   86 26 ″ ″  58  66  9 LPVCAFSSA ″ B*5501 100 ″   95 26 ″ ″  58  66  9 LPVCAFSSA ″ B*5601 100 ″   95 26 ″ ″  58  67 10 LPVCAFSSAG  987 B*3501  58 0,11    6 26 ″ ″  58  67 10 LPVCAFSSAG ″ B*3503   8 ″    1 26 ″ ″  58  67 10 LPVCAFSSAG ″ B*5501  19 ″    2 26 ″ ″ Cumulative Class 5422 I-BCI score^(E):  61  70 10 CAFSSAGPCA  988 A*3001  76 0,45   35 27  61  95  61  71 11 CAFSSAGPCAL  989 B*1402  57 1,74   99 27 ″ ″  61  71 11 CAFSSAGPCAL ″ B*3901  64 ″  111 27 ″ ″  61  71 11 CAFSSAGPCAL ″ B*4801  57 ″   99 27 ″ ″  63  71  9 FSSAGPCAL  990 B*3901 100 ″  174 27 ″ ″  63  71  9 FSSAGPCAL ″ B*4601  71 ″  124 27 ″ ″  62  72 11 AFSSAGPCALR  991 A*3101  40 1,24   50 27 ″ ″  63  72 10 FSSAGPCALR  992 A*3303  60 ″   74 27 ″ ″  63  72 10 FSSAGPCALR ″ A*6801 100 ″  124 27 ″ ″  64  72  9 SSAGPCALR  993 A*3303  87 ″  107 27 ″ ″  64  72  9 SSAGPCALR ″ A*6801  56 ″   69 27 ″ ″  63  73 11 FSSAGPCALRF  994 A*0101  38 1,58   59 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*1501  14 ″   23 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*1502  43 ″   68 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*1525  15 ″   24 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*3501  50 ″   79 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*4601  86 ″  136 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*5301  86 ″  136 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*5701  67 ″  105 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*5801 100 ″  158 27 ″ ″  63  73 11 FSSAGPCALRF ″ B*5802  50 ″   79 27 ″ ″  64  73 10 SSAGPCALRF  995 B*5802  20 ″   32 27 ″ ″  65  73  9 SAGPCALRF  996 A*0101  25 ″   40 27 ″ ″  65  73  9 SAGPCALRF ″ B*5701  17 ″   26 27 ″ ″  69  77  9 CALRFTSAR  997 A*3101  30 1,06   32 27 ″ ″  69  77  9 CALRFTSAR ″ A*3303 100 ″  106 27 ″ ″  69  77  9 CALRFTSAR ″ A*6801  11 ″   12 27 ″ ″  69  77  9 CALRFTSAR ″ A*7401 100 ″  106 27 ″ ″  70  77  8 ALRFTSAR  998 A*3001  18 ″   19 27 ″ ″  70  77  8 ALRFTSAR ″ A*3101  70 ″   74 27 ″ ″  70  77  8 ALRFTSAR ″ A*3303  53 ″   56 27 ″ ″  70  77  8 ALRFTSAR ″ A*7401  90 ″   95 27 ″ ″  70  77  8 ALRFTSAR ″ A*0301  81 ″   86 27 ″ ″  69  78 10 CALRFTSARR  999 A*3101  90 1,59  143 27 ″ ″  69  78 10 CALRFTSARR ″ A*3303  93 ″  148 27 ″ ″  69  78 10 CALRFTSARR ″ A*7401  60 ″   95 27 ″ ″  70  78  9 ALRFTSARR 1000 A*3101  20 ″   32 27 ″ ″  70  78  9 ALRFTSARR ″ A*3303   7 ″   11 27 ″ ″  70  78  9 ALRFTSARR ″ A*7401  80 ″  127 27 ″ ″  70  78  9 ALRFTSARR ″ A*0301  50 ″   80 27 ″ ″  71  78  8 LRFTSARR 1001 B*2705  10 ″   16 27 ″ ″  70  79 10 ALRFTSARRM 1002 B*0701  50 1,80   90 27 ″ ″  70  79 10 ALRFTSARRM ″ B*0801  67 ″  120 27 ″ ″  71  79  9 LRFTSARRM 1003 B*1402   7 ″   13 27 ″ ″  71  79  9 LRFTSARRM ″ B*2702  75 ″  135 27 ″ ″  71  79  9 LRFTSARRM ″ B*2705  60 ″  108 27 ″ ″  77  84  8 RRMETTVN 1004 B*2702  38 0,84   31 27 ″ ″  75  85 11 SARRMETTVNA 1005 A*3001   6 1,44    8 27 ″ ″  77  85  9 RRMETTVNA 1006 B*2702  50 ″   72 27 ″ ″  77  85  9 RRMETTVNA ″ B*2705  40 ″   58 27 ″ ″  77  86 10 RRMETTVNAH 1007 B*2702  63 0,74   46 27 ″ ″  79  86  8 METTVNAH 1008 A*6802  60 ″   44 27 ″ ″  79  86  8 METTVNAH ″ B*1801  67 ″   49 27 ″ ″  79  86  8 METTVNAH ″ B*4403  33 ″   25 27 ″ ″  77  87 11 RRMETTVNAHQ 1009 B*2702  25 0,30    7 27 ″ ″  79  87  9 METTVNAHQ 1010 B*4403  44 ″   13 27 ″ ″  78  88 11 RMETTVNAHQI 1011 A*3201  40 0,68   27 27 ″ ″  79  88 10 METTVNAHQI 1012 B*1301 100 ″   68 27 ″ ″  79  88 10 METTVNAHQI ″ B*1302  67 ″   45 27 ″ ″  79  88 10 METTVNAHQI ″ B*1801  33 ″   23 27 ″ ″  79  88 10 METTVNAHQI ″ B*3701 100 ″   68 27 ″ ″  79  88 10 METTVNAHQI ″ B*3801 100 ″   68 27 ″ ″  79  88 10 METTVNAHQI ″ B*4901 100 ″   68 27 ″ ″  79  88 10 METTVNAHQI ″ B*5001 100 ″   68 27 ″ ″  79  88 10 METTVNAHQI ″ B*5201 100 ″   68 27 ″ ″  80  88  9 ETTVNAHQI 1013 A*6802  40 ″   27 27 ″ ″  79  89 11 METTVNAHQIL 1014 B*1301  75 0,67   50 27 ″ ″  79  89 11 METTVNAHQIL ″ B*1801 100 ″   67 27 ″ ″  79  89 11 METTVNAHQIL ″ B*3701  92 ″   61 27 ″ ″  79  89 11 METTVNAHQIL ″ B*3801  80 ″   53 27 ″ ″  79  89 11 METTVNAHQIL ″ B*4001  90 ″   60 27 ″ ″  79  89 11 METTVNAHQIL ″ B*4002  43 ″   29 27 ″ ″  79  89 11 METTVNAHQIL ″ B*4402  40 ″   27 27 ″ ″  79  89 11 METTVNAHQIL ″ B*4403  67 ″   45 27 ″ ″  79  89 11 METTVNAHQIL ″ B*4801  43 ″   29 27 ″ ″  79  89 11 METTVNAHQIL ″ B*4901  78 ″   52 27 ″ ″  79  89 11 METTVNAHQIL ″ B*5001  20 ″   13 27 ″ ″  80  89 10 ETTVNAHQIL 1015 A*2501  40 ″   27 27 ″ ″  81  91 11 TTVNAHQILPK 1016 A*1101  67 0,39   26 27 ″ ″  81  91 11 TTVNAHQILPK ″ A*6801  44 ″   17 27 ″ ″  81  91 11 TTVNAHQILPK ″ A*0301   6 ″    2 27 ″ ″  82  91 10 TVNAHQILPK 1017 A*1101  92 ″   36 27 ″ ″  82  91 10 TVNAHQILPK ″ A*0301 100 ″   39 27 ″ ″  82  92 11 TVNAHQILPKV 1018 A*0201  27 1,32   36 27 ″ ″  84  93 10 NAHQILPKVL 1019 B*0701  25 1,59   40 27 ″ ″  85  93  9 AHQILPKVL 1020 B*3801  60 ″   95 27 ″ ″  85  93  9 AHQILPKVL ″ B*3901  18 ″   29 27 ″ ″  86  93  8 HQILPKVL 1021 B*3901  91 ″  144 27 ″ ″  86  93  8 HQILPKVL ″ B*4801 100 ″  159 27 ″ ″  86  95 10 HQILPKVLHK 1022 A*1101  42 1,60   67 27 ″ ″  86  95 10 HQILPKVLHK ″ A*0301  33 ″   53 27 ″ ″  87  95  9 QILPKVLHK 1023 A*1101  50 ″   80 27 ″ ″  87  95  9 QILPKVLHK ″ A*0101  75 ″  120 27 ″ ″  87  95  9 QILPKVLHK ″ A*0301 100 ″  160 27 ″ ″  88  95  8 ILPKVLHK 1024 A*0201  82 ″  131 27 ″ ″  88  95  8 ILPKVLHK ″ A*0301  63 ″  100 27 ″ ″   Cumulative Class 6468 I-BCI score:  86  93  8 HQILPKVL 1021 B*3901  91 ″  144 28  86 120  86  93  8 HQILPKVL ″ B*4801 100 ″  159 28 ″ ″  86  95 10 HQILPKVLHK 1022 A*1101  42 1,60   67 28 ″ ″  86  95 10 HQILPKVLHK ″ A*0301  33 ″   53 28 ″ ″  87  95  9 QILPKVLHK 1023 A*1101  50 ″   80 28 ″ ″  87  95  9 QILPKVLHK ″ A*0101  75 ″  120 28 ″ ″  87  95  9 QILPKVLHK ″ A*0301 100 ″  160 28 ″ ″  88  95  8 ILPKVLHK 1024 A*0201  82 ″  131 28 ″ ″  88  95  8 ILPKVLHK ″ A*0301  63 ″  100 28 ″ ″  86  96 11 HQILPKVLHKR 1025 A*3101  50 1,87   94 28 ″ ″  86  96 11 HQILPKVLHKR ″ A*3303  47 ″   87 28 ″ ″  87  96 10 QILPKVLHKR 1026 A*3101  60 ″  112 28 ″ ″  87  96 10 QILPKVLHKR ″ A*3303  67 ″  125 28 ″ ″  88  96  9 ILPKVLHKR 1027 A*3303  27 ″   50 28 ″ ″  88  96  9 ILPKVLHKR ″ A*0301  75 ″  141 28 ″ ″  89  96  8 LPKVLHKR 1028 B*0701  42 ″   78 28 ″ ″  88  97 10 ILPKVLHKRT 1029 A*0201  30 0,47   14 28 ″ ″  89  98 10 LPKVLHKRTL 1030 B*5101  64 1,61  103 28 ″ ″  89  98 10 LPKVIHKRTL ″ B*0701  88 ″  141 28 ″ ″  89  98 10 LPKVIHKRTL ″ B*0801 100 ″  161 28 ″ ″  91  98  8 KVLHKRTL 1031 B*0801  10 ″   16 28 ″ ″  91 100 10 KVLHKRTLGL 1032 A*0201  70 1,91  134 28 ″ ″  91 100 10 KVLHKRTLGL ″ B*0701  38 ″   72 28 ″ ″  91 100 10 KVLHKRTLGL ″ B*0801  33 ″   64 28 ″ ″  92 100  9 VLHKRTLGL 1033 A*0201  90 ″  172 28 ″ ″  92 100  9 VLHKRTLGL ″ B*0801 100 ″  191 28 ″ ″  92 102 11 VLHKRTLGLSA 1034 B*0801  70 1,09   76 28 ″ ″  95 102  8 KRTLGLSA 1035 B*2702  13 ″   14 28 ″ ″  93 103 11 LHKRTLGLSAM 1036 B*1402  86 1,72  148 28 ″ ″  93 103 11 LHKRTLGLSAM ″ B*0801  20 ″   34 28 ″ ″  94 103 10 HKRTLGLSAM 1037 B*1402  50 ″   86 28 ″ ″  95 103  9 KRTLGLSAM 1038 B*2702  88 ″  151 28 ″ ″  96 103  8 RTLGLSAM 1039 A*2501  20 ″   34 28 ″ ″  96 103  8 RTLGLSAM ″ A*3201 100 ″  172 28 ″ ″  96 103  8 RTLGLSAM ″ B*1502  29 ″   49 28 ″ ″  96 103  8 RTLGLSAM ″ B*1525  23 ″   40 28 ″ ″  96 103  8 RTLGLSAM ″ B*4601  93 ″  160 28 ″ ″  96 103  8 RTLGLSAM ″ B*5701  33 ″   57 28 ″ ″  96 103  8 RTLGLSAM ″ B*5801  80 ″  138 28 ″ ″  97 104  8 TLGLSAMS 1040 A*0201   9 0,51    5 28 ″ ″  97 105  9 TLGLAAMST 1041 A*0201  50 0,88   44 28 ″ ″  97 106 10 TLGLSAMSTT 1042 A*0201  40 0,27   11 28 ″ ″  99 108 10 GLSAMSTTDL 1043 A*0201  50 1,60   80 28 ″ ″ 100 110 11 LSAMSTTDLEA 1044 A*0206 100 1,07  107 28 ″ ″ 101 111 11 SAMSTTDLEAY 1045 A*2902  75 0,70   53 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ A*3002 100 ″   70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*1501 100 ″   70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*1502 100 ″   70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*1525 100 ″   70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*4601 100 ″   70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*5301  57 ″   40 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*5801  60 ″   42 28 ″ ″ 102 111 10 AMSTTDLEAY 1046 A*0301  50 ″   35 28 ″ ″ 103 111  9 MSTTDLEAY 1047 A*2601  25 ″   18 28 ″ ″ 103 111  9 MSTTDLEAY ″ A*0101  88 ″   62 28 ″ ″ 103 111  9 MSTTDLEAY ″ B*3501  83 ″   59 28 ″ ″ 104 111  8 STTDLEAY 1048 A*2501 100 ″   70 28 ″ ″ 102 112 11 AMSTTDLEAYF 1049 A*3002  20 1,45   29 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*1501  71 ″  104 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*1502  14 ″   21 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*1525  62 ″   89 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*4601   7 ″   10 28 ″ ″ 103 112 10 MSTTDLEAYF 1050 A*0101  13 ″   18 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*3501  42 ″   61 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*4601  43 ″   62 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*5301  14 ″   21 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*5802  40 ″   58 28 ″ ″ 104 112  9 STTDLEAYF 1051 A*2501  60 ″   87 28 ″ ″ 104 112  9 STTDLEAYF ″ A*2601  50 ″   73 28 ″ ″ 105 112  8 TTDLEAYF 1052 A*0101  75 ″  109 28 ″ ″ 103 113 11 MSTTDLEAYFK 1053 A*1101  75 0,43   32 28 ″ ″ 103 113 11 MSTTDLEAYFK ″ A*6801  67 ″   29 28 ″ ″ 104 113 10 STTDLEAYFK 1054 A*1101 100 ″   43 28 ″ ″ 104 113 10 STTDLEAYFK ″ A*6801  89 ″   38 28 ″ ″ 104 113 10 STTDLEAYFK ″ A*0301  19 ″    8 28 ″ ″ 105 113  9 TTDLEAYFK 1055 A*1101  83 ″   36 28 ″ ″ 105 113  9 TTDLEAYFK ″ A*6801  22 ″   10 28 ″ ″ 105 113  9 TTDLEAYFK ″ A*0101 100 ″   43 28 ″ ″ 105 113  9 TTDLEAYFK ″ A*0301  25 ″   11 28 ″ ″ 106 116 11 TDLEAYFKDCV 1056 A*0201  64 0,18   12 28 ″ ″ 106 116 11 TDLEAYFKDCV ″ B*3701  33 ″    6 28 ″ ″ 108 116  9 LEAYFKDCV 1057 A*0201  10 ″    2 28 ″ ″ 108 116  9 LEAYFKDCV ″ B*1301  25 ″    5 28 ″ ″ 108 116  9 LEAYFKDCV ″ B*3701  75 ″   14 28 ″ ″ 108 116  9 LEAYFKDCV ″ B*4001  40 ″    7 28 ″ ″ 108 116  9 LEAYFKDCV ″ B*4901  89 ″   16 28 ″ ″ 108 116  9 LEAYFKDCV ″ B*5001  80 ″   15 28 ″ ″ 109 116  8 EAYFKDCV 1058 B*0801  40 ″    7 28 ″ ″ 108 117 10 LEAYFKDCVF 1059 B*1301  63 1,37   85 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*3701  42 ″   57 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4001  20 ″   27 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4402  80 ″  109 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4403  89 ″  121 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4901  67 ″   91 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*5001  60 ″   82 28 ″ ″ 110 117  8 AYFKDCVF 1060 A*2301 100 ″  137 28 ″ ″ 110 117  8 AYFKDCVF ″ A*2402 100 ″  137 28 ″ ″ 109 118 10 EAYFKDCVFK 1061 A*1101  25 1,38   34 28 ″ ″ 109 118 10 EAYFKDCVFK ″ A*6801  78 ″  107 28 ″ ″ 110 118  9 AYFKDCVFK 1062 A*1101   8 ″   11 28 ″ ″ 111 118  8 YFKDCVFK 1063 A*3101  10 ″   14 28 ″ ″ 111 118  8 YFKDCVFK ″ A*3303  80 ″  110 28 ″ ″ 110 120 11 AYFKDCVFKDW 1064 A*2301  75 1,74  131 28 ″ ″ 110 120 11 AYFKDCVFKDW ″ A*2402  67 ″  116 28 ″ ″ Cumulative Class 7354 I-BCI score: 108 117 10 LEAYFKDCVF 1059 B*1301  63 1,37   85 29 108 141 108 117 10 LEAYFKDCVF ″ B*3701  42 ″   57 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4001  20 ″   27 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4402  80 ″  109 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4403  89 ″  121 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4901  67 ″   91 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*5001  60 ″   82 29 ″ ″ 110 117  8 AYFKDCVF 1060 A*2301 100 ″  137 29 ″ ″ 110 117  8 AYFKDCVF ″ A*2402 100 ″  137 29 ″ ″ 109 118 10 EAYFKDCVFK 1061 A*1101  25 1,38   34 29 ″ ″ 109 118 10 EAYFKDCVFK ″ A*6801  78 ″  107 29 ″ ″ 110 118  9 AYFKDCVFK 1062 A*1101   8 ″   11 29 ″ ″ 111 118  8 YFKDCVFK 1063 A*3101  10 ″   14 29 ″ ″ 111 118  8 YFKDCVFK ″ A*3303  80 ″  110 29 ″ ″ 110 120 11 AYFKDCVFKDW 1064 A*2301  75 1,74  131 29 ″ ″ 110 120 11 AYFKDCVFKDW ″ A*2402  67 ″  116 29 ″ ″ 114 123 10 DCVFKDWEEL 1065 A*3201  60 1,30   78 29 ″ ″ 115 123  9 CVFKDWEEL 1066 A*0201  40 ″   52 29 ″ ″ 115 123  9 CVFKDWEEL ″ B*0701  50 ″   65 29 ″ ″ 118 127 10 KDWEELGEEI 1067 B*1301  88 0,73   63 29 ″ ″ 118 127 10 KDWEELGEEI ″ B*1302 100 ″   73 29 ″ ″ 118 127 10 KDWEELGEEI ″ B*5201  67 ″   48 29 ″ ″ 120 127  8 WEELGEEI 1068 B*1301  50 ″   36 29 ″ ″ 120 127  8 WEELGEEI ″ B*4001  70 ″   51 29 ″ ″ 120 127  8 WEELGEEI ″ B*4901  56 ″   40 29 ″ ″ 119 129 11 DWEELGEEIRL 1069 A*0201  55 1,70   93 29 ″ ″ 120 129 10 WEELGEEIRL 1070 B*3801  20 ″   34 29 ″ ″ 120 129 10 WEELGEEIRL ″ B*4001  10 ″   17 29 ″ ″ 121 129  9 EELGEEIRL 1071 B*4001  60 ″  102 29 ″ ″ 121 129  9 EELGEEIRL ″ B*4403  22 ″   38 29 ″ ″ 121 131 11 EELGEEIRLKV 1072 B*1801  17 1,00   17 29 ″ ″ 121 131 11 EELGEEIRLKV ″ B*3701  50 ″   50 29 ″ ″ 122 131 10 ELGEEIRLKV 1073 A*0201  60 ″   60 29 ″ ″ 124 131  8 GEEIRLKV 1074 B*4901  11 ″   11 29 ″ ″ 123 132 10 LGEEIRLKVF 1075 A*0101  50 1,36   68 29 ″ ″ 124 132  9 GEEIRLKVF 1076 B*4402  60 ″   82 29 ″ ″ 124 132  9 GEEIRLKVF ″ B*4403  11 ″   15 29 ″ ″ 125 132  8 EEIRLKVF 1077 B*1801  83 ″  113 29 ″ ″ 125 132  8 EEIRLKVF ″ B*4402  20 ″   27 29 ″ ″ 125 132  8 EEIRLKVF ″ B*4403  56 ″   75 29 ″ ″ 123 133 11 LGEEIRLKVFV 1078 A*0206  50 1,07   54 29 ″ ″ 123 133 11 LGEEIRLKVFV ″ A*0201  91 ″   98 29 ″ ″ 125 133  9 EEIRLKVFV 1079 B*3701  58 ″   63 29 ″ ″ 125 133  9 EEIRLKVFV ″ B*4001  30 ″   32 29 ″ ″ 125 133  9 EEIRLKVFV ″ B*4403  78 ″   84 29 ″ ″ 126 133  8 EIRLKVFV 1080 B*0801 100 ″  107 29 ″ ″ 125 134 10 EEIRLKVFVL 1081 B*1801  50 1,85   93 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*3701  83 ″  154 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*3801  40 ″   74 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4001 100 ″  185 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4002  71 ″  132 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4402 100 ″  185 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4403 100 ″  185 29 ″ ″ 126 134  9 EIRLKVFVL 1082 B*0701  63 ″  116 29 ″ ″ 126 134  9 EIRLKVFVL ″ B*0801 100 ″  185 29 ″ ″ 127 134  8 IRLKVFVL 1083 A*0206  25 ″   46 29 ″ ″ 127 134  8 IRLKVFVL ″ B*1402  64 ″  119 29 ″ ″ 127 134  8 IRLKVFVL ″ B*2702 100 ″  185 29 ″ ″ 127 134  8 IRLKVFVL ″ B*3901  82 ″  151 29 ″ ″ 129 136  8 LKVFVLGG 1084 A*0206  75 0,47   35 29 ″ ″ 128 138 11 RLKVFVLGGCR 1085 A*3101  80 0,64   51 29 ″ ″ 128 138 11 RLKVFVLGGCR ″ A*7401  30 ″   19 29 ″ ″ 128 138 11 RLKVFVLGGCR ″ A*0301  13 ″    8 29 ″ ″ 130 138  9 KVFVLGGCR 1086 A*3101 100 ″   64 29 ″ ″ 130 138  9 KVFVLGGCR ″ A*7401  50 ″   32 29 ″ ″ 130 140 11 KVFVLGGCRHK 1087 A*1101  58 1,05   61 29 ″ ″ 130 140 11 KVFVLGGCRHK ″ A*3001  94 ″   99 29 ″ ″ 130 140 11 KVFVLGGCRHK ″ A*0301  94 ″   98 29 ″ ″ 133 140  8 VLGGCRHK 1088 A*0201  18 ″   19 29 ″ ″ 133 140  8 VLGGCRHK ″ A*0301  44 ″   46 29 ″ ″ 132 141 10 FVLGGCRHKL 1089 A*0201  80 1,66  133 29 ″ ″ 132 141 10 FVLGGCRHKL ″ B*0701  63 ″  104 29 ″ ″ 133 141  9 VLGGCRHKL 1090 A*0201 100 ″  166 29 ″ ″ Cumulative Class 5862 I-BCI score: “Start” and “End” are relative to the amino acid sequence of HBV X protein, consensus sequence, as depicted in SEQ ID NO: 45 ^(A)Peptide amino acid sequence. Each HLA class I binding peptide of HBV X protein is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods (Examples section). ^(C)C-score. See Material and Methods (Examples section). ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 6b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV X protein (consensus sequence). HLA class II binding peptides in SLP Peptide of derived from HBV X protein (consens. seq.) invention (SLP) SEQ HLA- Class ID DRB1 II-B SLP SLP Start End Sequence^(A) NO: molecule score^(B) SLP# Start End  46  60 PADHGAHLSLRGLPV 1091 *0701    8 26  36  68  47  61 ADHGAHLSLRGLPVC 1092 *0101   13 26 ″ ″  47  61 ADHGAHLSLRGLPVC ″ *0102   20 26 ″ ″  47  61 ADHGAHLSLRGLPVC ″ *0105   13 26 ″ ″  47  61 ADHGAHLSLRGLPVC ″ *0107   13 26 ″ ″  48  62 DHGAHLSLRGLPVCA 1093 *0101   87 26 ″ ″  48  62 DHGAHLSLRGLPVCA ″ *0102   67 26 ″ ″  48  62 DHGAHLSLRGLPVCA ″ *0104   43 26 ″ ″  48  62 DHGAHLSLRGLPVCA ″ *0105   87 26 ″ ″  48  62 DHGAHLSLRGLPVCA ″ *0106   53 26 ″ ″  48  62 DHGAHLSLRGLPVCA ″ *0107   87 26 ″ ″  49  63 HGAHLSLRGLPVCAF 1094 *0101  100 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *0102   93 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *0103   40 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *0104   90 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *0105   90 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *0106   90 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *0107   90 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *1101   85 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *1301  100 26 ″ ″  49  63 HGAHLSLRGLPVCAF ″ *1501   46 26 ″ ″  50  64 GAHLSLRGLPVCAFS 1095 *0101   77 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *0102   97 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *0103   70 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *0104   93 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *0105   93 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *0106   97 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *0107   93 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *1101   77 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *1301   92 26 ″ ″  50  64 GAHLSLRGLPVCAFS ″ *1501   54 26 ″ ″  51  65 AHLSLRGLPVCAFSS 1096 *0101  100 26 ″ ″  51  65 AHLSLRGLPVCAFSS ″ *0102  100 26 ″ ″  51  65 AHLSLRGLPVCAFSS ″ *0103  100 26 ″ ″  51  65 AHLSLRGLPVCAFSS ″ *0104  100 26 ″ ″  51  65 AHLSLRGLPVCAFSS ″ *0105  100 26 ″ ″  51  65 AHLSLRGLPVCAFSS ″ *0106  100 26 ″ ″  51  65 AHLSLRGLPVCAFSS ″ *0107  100 26 ″ ″  51  65 AHLSLRGLPVCAFSS ″ *1301   85 26 ″ ″  52  66 HLSLRGLPVCAFSSA 1097 *0101   97 26 ″ ″  52  66 HLSLRGLPVCAFSSA ″ *0102   90 26 ″ ″  52  66 HLSLRGLPVCAFSSA ″ *0103   90 26 ″ ″  52  66 HLSLRGLPVCAFSSA ″ *0104   97 26 ″ ″  52  66 HLSLRGLPVCAFSSA ″ *0105   97 26 ″ ″  52  66 HLSLRGLPVCAFSSA ″ *0106   93 26 ″ ″  52  66 HLSLRGLPVCAFSSA ″ *0107   97 26 ″ ″  52  66 HLSLRGLPVCAFSSA ″ *1301   77 26 ″ ″  53  67 LSLRGLPVCAFSSAG 1098 *0101   83 26 ″ ″  53  67 LSLRGLPVCAFSSAG ″ *0102   50 26 ″ ″  53  67 LSLRGLPVCAFSSAG ″ *0104   77 26 ″ ″  53  67 LSLRGLPVCAFSSAG ″ *0105   83 26 ″ ″  53  67 LSLRGLPVCAFSSAG ″ *0106   73 26 ″ ″  53  67 LSLRGLPVCAFSSAG ″ *0107   83 26 ″ ″  53  67 LSLRGLPVCAFSSAG ″ *1301   69 26 ″ ″  54  68 SLRGLPVCAFSSAGP 1099 *0101   37 26 ″ ″  54  68 SLRGLPVCAFSSAGP ″ *0102    7 26 ″ ″  54  68 SLRGLPVCAFSSAGP ″ *0104   30 26 ″ ″  54  68 SLRGLPVCAFSSAGP ″ *0105   37 26 ″ ″  54  68 SLRGLPVCAFSSAGP ″ *0106    7 26 ″ ″  54  68 SLRGLPVCAFSSAGP ″ *0107   37 26 ″ ″  54  68 SLRGLPVCAFSSAGP ″ *1301   62 26 ″ ″ Cumulative Class II-B score^(C): 4414  61  75 CAFSSAGPCALRFTS 1100 *0101   20 27  61  95  61  75 CAFSSAGPCALRFTS ″ *0105   20 27 ″ ″  61  75 CAFSSAGPCALRFTS ″ *0107   20 27 ″ ″  61  75 CAFSSAGPCALRFTS ″ *0701   15 27 ″ ″  64  78 SSAGPCALRFTSARR 1101 *1501   69 27 ″ ″  65  79 SAGPCALRFTSARRM 1102 *0101   23 27 ″ ″  65  79 SAGPCALRFTSARRM ″ *0102   23 27 ″ ″  65  79 SAGPCALRFTSARRM ″ *0104   27 27 ″ ″  65  79 SAGPCALRFTSARRM ″ *0106   23 27 ″ ″  65  79 SAGPCALRFTSARRM ″ *0401   31 27 ″ ″  65  79 SAGPCALRFTSARRM ″ *0701   85 27 ″ ″  65  79 SAGPCALRFTSARRM ″ *1301   46 27 ″ ″  65  79 SAGPCALRFTSARRM ″ *1501   92 27 ″ ″  66  80 AGPCALRFTSARRME 1103 *0101   69 27 ″ ″  66  80 AGPCALRFTSARRME ″ *0102   37 27 ″ ″  66  80 AGPCALRFTSARRME ″ *0104   40 27 ″ ″  66  80 AGPCALRFTSARRME ″ *0105    3 27 ″ ″  66  80 AGPCALRFTSARRME ″ *0106   37 27 ″ ″  66  80 AGPCALRFTSARRME ″ *0107    3 27 ″ ″  66  80 AGPCALRFTSARRME ″ *0401   46 27 ″ ″  66  80 AGPCALRFTSARRME ″ *0701   69 27 ″ ″  66  80 AGPCALRFTSARRME ″ *1301   38 27 ″ ″  66  80 AGPCALRFTSARRME ″ *1501   85 27 ″ ″  67  81 GPCALRFTSARRMET 1104 *0101   62 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0102   57 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0104   70 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0105   43 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0106   80 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0107   43 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0301   46 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0401   92 27 ″ ″  67  81 GPCALRFTSARRMET ″ *0701   77 27 ″ ″  67  81 GPCALRFTSARRMET ″ *1101    8 27 ″ ″  67  81 GPCALRFTSARRMET ″ *1301   31 27 ″ ″  67  81 GPCALRFTSARRMET ″ *1501  100 27 ″ ″  68  82 PCALRFTSARRMETT 1105 *0101   54 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0102   60 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0104   83 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0105   57 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0106   83 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0107   57 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0301   38 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0401   69 27 ″ ″  68  82 PCALRFTSARRMETT ″ *0701  100 27 ″ ″  68  82 PCALRFTSARRMETT ″ *1101   31 27 ″ ″  68  82 PCALRFTSARRMETT ″ *1301   23 27 ″ ″  68  82 PCALRFTSARRMETT ″ *1501   77 27 ″ ″  69  83 CALRFTSARRMETTV 1106 *0101   46 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0102   43 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0104   67 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0105   47 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0106   57 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0107   47 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0301   31 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0401   23 27 ″ ″  69  83 CALRFTSARRMETTV ″ *0701   92 27 ″ ″  69  83 CALRFTSARRMETTV ″ *1101   38 27 ″ ″  69  83 CALRFTSARRMETTV ″ *1301   15 27 ″ ″  69  83 CALRFTSARRMETTV ″ *1501   62 27 ″ ″  70  84 ALRFTSARRMETTVN 1107 *0101   38 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *0102   17 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *0104   37 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *0106    3 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *0301   62 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *0401    8 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *0701   62 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *1101   46 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *1301    8 27 ″ ″  70  84 ALRFTSARRMETTVN ″ *1501   23 27 ″ ″  71  85 LRFTSARRMETTVNA 1108 *0301   23 27 ″ ″  71  85 LRFTSARRMETTVNA ″ *0401   15 27 ″ ″  71  85 LRFTSARRMETTVNA ″ *0701   54 27 ″ ″  71  85 LRFTSARRMETTVNA ″ *1101   23 27 ″ ″  73  87 FTSARRMETTVNAHQ 1109 *0401   85 27 ″ ″  74  88 TSARRMETTVNAHQI 1110 *0401  100 27 ″ ″  75  89 SARRMETTVNAHQIL 1111 *0401   38 27 ″ ″  75  89 SARRMETTVNAHQIL ″ *1301   40 27 ″ ″  76  90 ARRMETTVNAHQILP 1112 *0401   80 27 ″ ″  76  90 ARRMETTVNAHQILP ″ *1301   10 27 ″ ″  77  91 RRMETTVNAHQILPK 1113 *1301   50 27 ″ ″  78  92 RMETTVNAHQILPKV 1114 *1301   20 27 ″ ″  81  95 TTVNAHQILPKVLHK 1115 *1101   15 27 ″ ″ Cumulative Class II-B score: 3788  86 100 HQILPKVLHKRTLGL 1116 *1101   54 28  86 120  87 101 QILPKVLHKRTLGLS 1117 *0102   10 28 ″ ″  87 101 QILPKVLHKRTLGLS ″ *1101   22 28 ″ ″  87 101 QILPKVLHKRTLGLS ″ *1301   70 28 ″ ″  88 102 ILPKVLHKRTLGLSA 1118 *0102   53 28 ″ ″  88 102 ILPKVLHKRTLGLSA ″ *0104   17 28 ″ ″  88 102 ILPKVLHKRTLGLSA ″ *0106   33 28 ″ ″  88 102 ILPKVLHKRTLGLSA ″ *1101   44 28 ″ ″  88 102 ILPKVLHKRTLGLSA ″ *1301   80 28 ″ ″  89 103 LPKVLHKRTLGLSAM 1119 *0101   10 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *0102   77 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *0104   60 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *0105   10 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *0106   77 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *0107   10 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *0701   10 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *1101   78 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *1301  100 28 ″ ″  89 103 LPKVLHKRTLGLSAM ″ *1501   40 28 ″ ″  90 104 PKVLHKRTLGLSAMS 1120 *0101   33 28 ″ ″  90 104 PKVLHKRTLGLSAMS ″ *0102   73 28 ″ ″  90 104 PKVLHKRTLGLSAMS ″ *0104   63 28 ″ ″  90 104 PKVLHKRTLGLSAMS ″ *0105   33 28 ″ ″  90 104 PKVLHKRTLGLSAMS ″ *0106   67 28 ″ ″  90 104 PKVLHKRTLGLSAMS ″ *0107   33 28 ″ ″  90 104 PKVLHKRTLGLSAMS ″ *1101   72 28 ″ ″  90 104 PKVLHKRTLGLSAMS ″ *1301   90 28 ″ ″  91 105 KVLHKRTLGLSAMST 1121 *0101   63 28 ″ ″  91 105 KVLHKRTLGLSAMST ″ *0102   70 28 ″ ″  91 105 KVLHKRTLGLSAMST ″ *0104   50 28 ″ ″  91 105 KVLHKRTLGLSAMST ″ *0105   63 28 ″ ″  91 105 KVLHKRTLGLSAMST ″ *0106   60 28 ″ ″  91 105 KVLHKRTLGLSAMST ″ *0107   63 28 ″ ″  91 105 KVLHKRTLGLSAMST ″ *1101   11 28 ″ ″  91 105 KVLHKRTLGLSAMST ″ *1301   60 28 ″ ″  92 106 VLHKRTLGLSAMSTT 1122 *0101   15 28 ″ ″  92 106 VLHKRTLGLSAMSTT ″ *0102   47 28 ″ ″  92 106 VLHKRTLGLSAMSTT ″ *0104   23 28 ″ ″  92 106 VLHKRTLGLSAMSTT ″ *0105   73 28 ″ ″  92 106 VLHKRTLGLSAMSTT ″ *0106   43 28 ″ ″  92 106 VLHKRTLGLSAMSTT ″ *0107   73 28 ″ ″  93 107 LHKRTLGLSAMSTTD 1123 *0101   60 28 ″ ″  93 107 LHKRTLGLSAMSTTD ″ *0102   27 28 ″ ″  93 107 LHKRTLGLSAMSTTD ″ *0105   60 28 ″ ″  93 107 LHKRTLGLSAMSTTD ″ *0107   60 28 ″ ″  94 108 HKRTLGLSAMSTTDL 1124 *0101   92 28 ″ ″  94 108 HKRTLGLSAMSTTDL ″ *0102   33 28 ″ ″  94 108 HKRTLGLSAMSTTDL ″ *0104    3 28 ″ ″  94 108 HKRTLGLSAMSTTDL ″ *0105   67 28 ″ ″  94 108 HKRTLGLSAMSTTDL ″ *0106   40 28 ″ ″  94 108 HKRTLGLSAMSTTDL ″ *0107   67 28 ″ ″  94 108 HKRTLGLSAMSTTDL ″ *0401   77 28 ″ ″  95 109 KRTLGLSAMSTTDLE 1125 *0101   31 28 ″ ″  95 109 KRTLGLSAMSTTDLE ″ *0105   23 28 ″ ″  95 109 KRTLGLSAMSTTDLE ″ *0106   17 28 ″ ″  95 109 KRTLGLSAMSTTDLE ″ *0107   23 28 ″ ″  95 109 KRTLGLSAMSTTDLE ″ *0401   54 28 ″ ″  96 110 RTLGLSAMSTTDLEA 1126 *0101    8 28 ″ ″  96 110 RTLGLSAMSTTDLEA ″ *0105   30 28 ″ ″  96 110 RTLGLSAMSTTDLEA ″ *0106   27 28 ″ ″  96 110 RTLGLSAMSTTDLEA ″ *0107   30 28 ″ ″  96 110 RTLGLSAMSTTDLEA ″ *0401   62 28 ″ ″  97 111 TLGLSAMSTTDLEAY 1127 *0101   17 28 ″ ″  97 111 TLGLSAMSTTDLEAY ″ *0105   17 28 ″ ″  97 111 TLGLSAMSTTDLEAY ″ *0106   20 28 ″ ″  97 111 TLGLSAMSTTDLEAY ″ *0107   17 28 ″ ″  97 111 TLGLSAMSTTDLEAY ″ *0401   50 28 ″ ″ 105 119 TTDLEAYFKDCVFKD 1128 *0301   69 28 ″ ″ 106 120 TDLEAYFKDCVFKDW 1129 *0301   54 28 ″ ″ Cumulative Class II-B score: 3170 108 122 LEAYFKDCVFKDWEE 1130 *0301   15 29 108 141 110 124 AYFKDCVFKDWEELG 1131 *0301  100 29 ″ ″ 111 125 YFKDCVFKDWEELGE 1132 *0301   92 29 ″ ″ 119 133 DWEELGEEIRLKVFV 1133 *0301   77 29 ″ ″ 120 134 WEELGEEIRLKVFVL 1134 *0301   85 29 ″ ″ 120 134 WEELGEEIRLKVFVL ″ *1501    8 29 ″ ″ 121 135 EELGEEIRLKVFVLG 1135 *1501   31 29 ″ ″ 123 137 LGEEIRLKVFVLGGC 1136 *1501   15 29 ″ ″ 124 138 GEEIRLKVFVLGGCR 1137 *1501   38 29 ″ ″ 125 139 EEIRLKVFVLGGCRH 1138 *0102    3 29 ″ ″ 126 140 EIRLKVFVLGGCRHK 1139 *0102   40 29 ″ ″ 126 140 EIRLKVFVLGGCRHK ″ *0104   20 29 ″ ″ 126 140 EIRLKVFVLGGCRHK ″ *1501   10 29 ″ ″ 127 141 IRLKVFVLGGCRHKL 1140 *0101   40 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0102   80 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0104   73 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0105   40 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0106   70 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0107   40 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *1101   56 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *1501   90 29 ″ ″ Cumulative Class II-B score: 1024 “Start” and “End” are relative to the amino acid sequence of human HBV X protein as depicted in SEQ ID NO: 45 ^(A)Peptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV X protein is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)Class II-B score. See Material and Methods (Examples section). ^(C)Cumulative Class II-B score. See Material and Methods (Examples section).

TABLE 7a Predicted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences from HBV large surface protein. HLA class I binding peptides contained in Peptide of SLP sequences derived from HBV Surface antigen invention (SLP) SEQ HLA Class Class ID class 1 I-B I-BCI SLP SLP Start End Length Sequence^(A) NO: molecule score^(B) C-score^(C) score^(D) SLP# Start End 175 182  8 MENITSGF 1146 B*4901  40 1,40    56  30 175 210 175 182  8 MENITSGF ″ B*5001  35 1,40    49 ″ ″ ″ 175 182  8 MENITSGF ″ B*1801  30 1,40    42 ″ ″ ″ 175 183  9 MENITSGFL 1147 B*4403  90 0,93    84 ″ ″ ″ 175 183  9 MENITSGFL ″ B*4402  85 0,93    79 ″ ″ ″ 175 183  9 MENITSGFL ″ B*4001  75 0,93    70 ″ ″ ″ 175 183  9 MENITSGFL ″ B*5001  25 0,93    23 ″ ″ ″ 175 183  9 MENITSGFL ″ B*4901  20 0,93    19 ″ ″ ″ 175 184 10 MENITSGFLG 1148 B*4402  75 0,59    44 ″ ″ ″ 175 184 10 MENITSGFLG ″ B*4403  60 0,59    35 ″ ″ ″ 175 185 11 MENITSGFLGP 1149 B*4402  35 0,19     7 ″ ″ ″ 175 186 12 MENITSGFLGPL 1150 B*4001  90 0,80    72 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4002  80 0,80    64 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4402  80 0,80    64 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4403  80 0,80    64 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*1801  70 0,80    56 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*3701  60 0,80    48 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*5001  55 0,80    44 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4901  30 0,80    24 ″ ″ ″ 176 186 11 ENITSGFLGPL 1151 A*6802  20 0,80    16 ″ ″ ″ 175 187 13 MENITSGFLGPLL 1152 B*4402  95 0,77    73 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4403  95 0,77    73 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4001  85 0,77    66 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*5001  75 0,77    58 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*3701  70 0,77    54 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4002  65 0,77    50 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4901  60 0,77    46 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*1801  40 0,77    31 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*1301  25 0,77    19 ″ ″ ″ 178 187 10 ITSGFLGPLL 1153 A*3001  15 0,77    12 ″ ″ ″ 175 188 14 MENITSGFLGPLLV 1154 B*4901  95 1,48   141 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4402  90 1,48   133 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4403  85 1,48   126 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*5001  80 1,48   119 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4001  65 1,48    96 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*3701  50 1,48    74 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4002  10 1,48    15 ″ ″ ″ 182 193 12 FLGPLLVLQAGF 1155 B*1501  30 1,17    35 ″ ″ ″ 186 193  8 LLVLQAGF 1156 B*1501  10 1,17    12 ″ ″ ″ 187 194  8 LVLQAGFF 1157 A*2601  15 0,99    15 ″ ″ ″ 182 195 14 FLGPLLVLQAGFFL 1158 A*0201  63 1,59   100 ″ ″ ″ 182 195 14 FLGPLLVLQAGFFL ″ A*0206  55 1,59    87 ″ ″ ″ 186 195 10 LLVLqAGFFL 1159 A*0201  66 1,59   104 ″ ″ ″ 187 195  9 LVLQAGFFL 1160 A*0201  20 1,59    32 ″ ″ ″ 187 196 10 LVLQAGFFLL 1161 A*0206  20 1,85    37 ″ ″ ″ 188 196  9 VLQAGFFLL 1162 A*0201  26 1,85    48 ″ ″ ″ 189 196  8 LQAGFFLL 1163 B*3701  85 1,85   157 ″ ″ ″ 189 196  8 LQAGFFLL ″ B*4801  60 1,85   111 ″ ″ ″ 189 196  8 LQAGFFLL ″ B*1301  50 1,85    92 ″ ″ ″ 189 196  8 LQAGFFLL ″ B*3901  45 1,85    83 ″ ″ ″ 189 196  8 LQAGFFLL ″ B*1302  40 1,85    74 ″ ″ ″ 189 196  8 LQAGFFLL ″ B*3801  35 1,85    65 ″ ″ ″ 189 196  8 LQAGFFLL ″ B*5001  30 1,85    55 ″ ″ ″ 187 198 12 LVLQAGFFLLTR 1164 A*7401  30 1,36    41 ″ ″ ″ 187 198 12 LVLQAGFFLLTR ″ A*3101  10 1,36    14 ″ ″ ″ 187 198 12 LVLQAGFFLLTR ″ A*1101   5 1,36     7 ″ ″ ″ 188 198 11 VLQAGFFLLTR 1165 A*7401  90 1,36   122 ″ ″ ″ 189 198 10 LQAGFFLLTR 1166 A*3101  80 1,36   109 ″ ″ ″ 189 198 10 LQAGFFLLTR ″ A*7401  65 1,36    88 ″ ″ ″ 189 198 10 LQAGFFLLTR ″ A*1101  15 1,36    20 ″ ″ ″ 190 198  9 QAGFFLLTR 1167 A*7401  10 1,36    14 ″ ″ ″ 191 198  8 AGFFLLTR 1168 A*7401  70 1,36    95 ″ ″ ″ 189 199 11 LQAGFFLLTRI 1169 B*5201  95 1,36   129 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*1302  85 1,36   115 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*4901  50 1,36    68 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*1301  30 1,36    41 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*4001  25 1,36    34 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*5001  15 1,36    20 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*3701  10 1,36    14 ″ ″ ″ 189 200 12 LQAGFFLLTRIL 1170 B*4001  60 1,90   114 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*3701  40 1,90    76 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*4801  40 1,90    76 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*3901  30 1,90    57 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*5001   5 1,90     9 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI 1171 B*5201  80 1,73   139 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*4901  65 1,73   113 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*5001  65 1,73   113 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*1301  60 1,73   104 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*1302  55 1,73    95 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ A*0206  50 1,73    87 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*3701  45 1,73    78 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*4001  45 1,73    78 ″ ″ ″ 191 202 12 AGFFLLTRILTI 1172 B*5201  50 1,73    87 ″ ″ ″ 194 202  9 FLLTRILTI 1173 B*0801  80 1,73   139 ″ ″ ″ 194 202  9 FLLTRILTI ″ A*0201  37 1,73    64 ″ ″ ″ 194 206 13 FLLTRILTIPQSL 1174 B*0801 100 1,23   123 ″ ″ ″ 194 206 13 FLLTRILTIPQSL ″ A*0201  29 1,23    35 ″ ″ ″ 195 206 12 LLTRILTIPQSL 1175 B*1402  70 1,23    86 ″ ″ ″ 196 206 11 LTRILTIPQSL 1176 A*3001  25 1,23    31 ″ ″ ″ 196 206 11 LTRILTIPQSL ″ B*1402  10 1,23    12 ″ ″ ″ 197 206 10 TRILTIPQSL 1177 B*3901 100 1,23   123 ″ ″ ″ 197 206 10 TRILTIPQSL ″ B*2705   5 1,23     6 ″ ″ ″ 196 209 14 LTRILTIPQSLDSW 1178 B*5701  75 1,47   111 ″ ″ ″ 196 209 14 LTRILTIPQSLDSW ″ B*5802  40 1,47    59 ″ ″ ″ 198 209 12 RILTIPQSLDSW 1179 B*5801  65 1,47    96 ″ ″ ″ 198 209 12 RILTIPQSLDSW ″ A*3201  60 1,47    88 ″ ″ ″ 198 209 12 RILTIPQSLDSW ″ B*5701  50 1,47    74 ″ ″ ″ 200 209 10 LTIPQSLDSW 1180 B*5802  90 1,47   133 ″ ″ ″ 200 209 10 LTIPQSLDSW ″ A*2501  40 1,47    59 ″ ″ ″ 197 210 14 TRILTIPQSLDSWW 1181 B*4402  20 0,79    16 ″ ″ ″ 197 210 14 TRILTIPQSLDSWW ″ B*4403  15 0,79    12 ″ ″ ″ 198 210 13 RILTIPQSLDSWW 1182 B*5801  60 0,79    47 ″ ″ ″ 198 210 13 RILTIPQSLDSWW ″ B*5701  40 0,79    31 ″ ″ ″ 200 210 11 LTIPQSLDSWW 1183 B*5802  75 0,79    59 ″ ″ ″ 200 210 11 LTIPQSLDSWW ″ B*5801  40 0,79    31 ″ ″ ″ 202 210  9 IPQSLDSWW 1184 B*5301  50 0,79    39 ″ ″ ″ Cumulative Class  6882 I-BCI score: 239 246  8 CPPICPGY 1185 B*3501  45 1,44    65  31 239 274 239 248 10 CPPICPGYRW 1186 B*5301  85 1,94   165 ″ ″ ″ 240 251 12 PPICPGYRWMCL 1187 B*3503  50 1,46    73 ″ ″ ″ 243 251  9 CPGYRWMCL 1188 B*0801  75 1,46   110 ″ ″ ″ 243 251  9 CPGYRWMCL ″ B*1402  50 1,46    73 ″ ″ ″ 243 252 10 CPGYRWMCLR 1189 A*3303   5 1,04     5 ″ ″ ″ 244 252  9 PGYRWMCLR 1190 A*3101   5 1,04     5 ″ ″ ″ 245 252  8 GYRWMCLR 1191 A*3101  95 1,04    99 ″ ″ ″ 245 252  8 GYRWMCLR ″ A*3303  10 1,04    10 ″ ″ ″ 245 253  9 GYRWMCLRR 1192 A*3101  45 0,95    43 ″ ″ ″ 245 254 10 GYRWMCLRRF 1193 A*2402  10 1,01    10 ″ ″ ″ 246 254  9 YRWMCLRRF 1194 B*2702  40 1,01    41 ″ ″ ″ 246 254  9 YRWMCLRRF ″ B*2705  40 1,01    41 ″ ″ ″ 245 255 11 GYRWMCLRRFI 1195 A*3001  35 0,99    35 ″ ″ ″ 246 255 10 YRWMCLRRFI 1196 B*1402  90 0,99    89 ″ ″ ″ 246 255 10 YRWMCLRRFI ″ B*2702  85 0,99    84 ″ ″ ″ 246 255 10 YRWMCLRRFI ″ B*2705  20 0,99    20 ″ ″ ″ 243 256 14 CPGYRWMCLRRFII 1197 B*0801  65 0,86    56 ″ ″ ″ 243 256 14 CPGYRWMCLRRFII ″ B*5101  25 0,86    21 ″ ″ ″ 246 256 11 YRWMCLRRFII 1198 B*2702 100 0,86    86 ″ ″ ″ 246 256 11 YRWMCLRRFII ″ B*1402  75 0,86    64 ″ ″ ″ 246 256 11 YRWMCLRRFII ″ B*2705  65 0,86    56 ″ ″ ″ 246 256 11 YRWMCLRRFII ″ B*3801  60 0,86    51 ″ ″ ″ 247 256 10 RWMCLRRFII 1199 A*2402  55 0,86    47 ″ ″ ″ 247 256 10 RWMCLRRFII ″ A*2301  35 0,86    30 ″ ″ ″ 245 257 13 GYRWMCLRRFIIF 1200 A*2301  85 1,08    92 ″ ″ ″ 246 257 12 YRWMCLRRFIIF 1201 B*1402 100 1,08   108 ″ ″ ″ 246 257 12 YRWMCLRRFIIF ″ B*2702  75 1,08    81 ″ ″ ″ 246 257 12 YRWMCLRRFIIF ″ B*2705  60 1,08    65 ″ ″ ″ 247 257 11 RWMCLRRFIIF 1202 A*2402  50 1,08    54 ″ ″ ″ 249 257  9 MCLRRFIIF 1203 B*0801  55 1,08    59 ″ ″ ″ 245 258 14 GYRWMCLRRFIIFL 1204 A*3001  45 1,61    72 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL 1205 B*1402  95 1,61   153 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL ″ B*2705  85 1,61   137 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL ″ B*2702  60 1,61    96 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL ″ B*3801  20 1,61    32 ″ ″ ″ 249 258 10 MCLRRFIIFL 1206 B*0801  15 1,61    24 ″ ″ ″ 251 258  8 LRRFIIFL 1207 B*1402  60 1,61    96 ″ ″ ″ 246 259 14 YRWMCLRRFIIFLF 1208 B*2702  55 1,73    95 ″ ″ ″ 246 259 14 YRWMCLRRFIIFLF ″ B*2705  45 1,73    78 ″ ″ ″ 246 259 14 YRWMCLRRFIIFLF ″ B*3801  40 1,73    69 ″ ″ ″ 247 259 13 RWMCLRRFIIFLF 1209 A*2402 100 1,73   173 ″ ″ ″ 247 259 13 RWMCLRRFIIFLF ″ A*2301  80 1,73   138 ″ ″ ″ 249 259 11 MCLRRFIIFLF 1210 B*1801  50 1,73    86 ″ ″ ″ 251 259  9 LRRFIIFLF 1211 B*2705  25 1,73    43 ″ ″ ″ 252 259  8 RRFIIFLF 1212 B*2702  90 1,73   155 ″ ″ ″ 252 259  8 RRFIIFLF ″ B*2705  70 1,73   121 ″ ″ ″ 252 259  8 RRFIIFLF ″ B*3801  70 1,73   121 ″ ″ ″ 247 260 14 RWMCLRRFIIFLFI 1213 A*2402  65 1,60   104 ″ ″ ″ 248 260 13 WMCLRRFIIFLFI 1214 B*0801   5 1,60     8 ″ ″ ″ 249 260 12 MCLRRFIIFLFI 1215 B*0801  90 1,60   144 ″ ″ ″ 250 260 11 CLRRFIIFLFI 1216 A*3001  60 1,60    96 ″ ″ ″ 251 260 10 LRRFIIFLFI 1217 B*1402  25 1,60    40 ″ ″ ″ 252 260  9 RRFIIFLFI 1218 B*2705  75 1,60   120 ″ ″ ″ 252 260  9 RRFIIFLFI ″ B*3801  50 1,60    80 ″ ″ ″ 252 260  9 RRFIIFLFI ″ B*2702  35 1,60    56 ″ ″ ″ 248 261 14 WMCLRRFIIFLFIL 1219 B*0801  20 1,79    36 ″ ″ ″ 249 261 13 MCLRRFIIFLFIL 1220 B*0801  70 1,79   126 ″ ″ ″ 250 261 12 CLRRFIIFLFIL 1221 B*0801  25 1,79    45 ″ ″ ″ 251 261 11 LRRFIIFLFIL 1222 B*1402  35 1,79    63 ″ ″ ″ 252 261 10 RRFIIFLFIL 1223 B*2705 100 1,79   179 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*3801  85 1,79   152 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*2702  80 1,79   144 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*4801  50 1,79    90 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*4001  10 1,79    18 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*4002   5 1,79     9 ″ ″ ″ 253 261  9 RFIIFLFIL 1224 B*4001  15 1,79    27 ″ ″ ″ 254 261  8 FIIFLFIL 1225 A*2501  10 1,79    18 ″ ″ ″ 249 262 14 MCLRRFIIFLFILL 1226 B*0801  60 1,50    90 ″ ″ ″ 250 262 13 CLRRFIIFLFILL 1227 A*3001   5 1,50     7 ″ ″ ″ 251 262 12 LRRFIIFLFILL 1228 B*2705  35 1,50    52 ″ ″ ″ 251 262 12 LRRFIIFLFILL ″ B*1402   5 1,50     7 ″ ″ ″ 252 262 11 RRFIIFLFILL 1229 B*2702  95 1,50   142 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*2705  95 1,50   142 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*3801  80 1,50   120 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*4002  60 1,50    90 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*4801  45 1,50    67 ″ ″ ″ 253 262 10 RFIIFLFILL 1230 B*4001  20 1,50    30 ″ ″ ″ 254 262  9 FIIFLFILL 1231 A*6802  60 1,50    90 ″ ″ ″ 254 262  9 FIIFLFILL ″ A*2601  30 1,50    45 ″ ″ ″ 251 263 13 LRRFIIFLFILLL 1232 B*2705  50 1,90    95 ″ ″ ″ 252 263 12 RRFIIFLFILLL 1233 B*2705  90 1,90   171 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*3801  90 1,90   171 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*2702  70 1,90   133 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*4002  40 1,90    76 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*4801   5 1,90    10 ″ ″ ″ 254 263 10 FIIFLFILLL 1234 A*2601  65 1,90   124 ″ ″ ″ 252 264 13 RRFIIFLFILLLC 1235 B*2705  30 0,75    22 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL 1236 B*2705  80 1,60   128 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL ″ B*2702  50 1,60    80 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL ″ B*4002  25 1,60    40 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL ″ B*3801  10 1,60    16 ″ ″ ″ 257 265  9 FLFILLLCL 1237 A*0201  60 1,60    96 ″ ″ ″ 254 266 13 FIIFLFILLLCLI 1238 A*6802  40 0,76    30 ″ ″ ″ 257 266 10 FLFIILLCLI 1239 A*0201  31 0,76    24 ″ ″ ″ 257 266 10 FLFILLLCLI ″ B*5101  15 0,76    11 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF 1240 A*2501  80 1,24    99 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ A*2601  70 1,24    86 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ B*1501  50 1,24    62 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ B*4601  35 1,24    43 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ A*2902  20 1,24    25 ″ ″ ″ 255 267 13 IIFLFILLLCLIF 1241 A*3201  20 1,24    25 ″ ″ ″ 256 267 12 IFLFILLLCLIF 1242 A*2301  95 1,24   117 ″ ″ ″ 256 267 12 IFLFILLLCLIF ″ A*2902  30 1,24    37 ″ ″ ″ 257 267 11 FLFILLLCLIF 1243 B*4601  80 1,24    99 ″ ″ ″ 257 267 11 FLFILLLCLIF ″ B*1501  65 1,24    80 ″ ″ ″ 257 267 11 FLFILLLCLIF ″ B*1502  65 1,24    80 ″ ″ ″ 258 267 10 LFILLLCLIF 1244 A*2301  50 1,24    62 ″ ″ ″ 256 268 13 IFLFILLLCLIFL 1245 A*2301  10 1,44    14 ″ ″ ″ 257 268 12 FLFILLLCLIFL 1246 A*0201  40 1,44    57 ″ ″ ″ 259 268 10 FILLICLIFL 1247 A*0201  49 1,44    70 ″ ″ ″ 259 268 10 FILLLCLIFL ″ A*0206   5 1,44     7 ″ ″ ″ 260 268  9 ILLLCLIFL 1248 A*0201  71 1,44   103 ″ ″ ″ 256 269 14 IFLFILLLCLIFLL 1249 A*2301  65 1,83   119 ″ ″ ″ 257 269 13 FLFILLLCLIFLL 1250 A*0201  23 1,83    42 ″ ″ ″ 260 269 10 ILLLcLIFLL 1251 A*0201  77 1,83   141 ″ ″ ″ 261 269  9 LLLCLIFLL 1252 A*0201  83 1,83   152 ″ ″ ″ 259 270 12 FILLLCLIFLLV 1253 A*0206  40 1,71    68 ″ ″ ″ 260 270 11 ILLLCLIFLLV 1254 A*0206  45 1,71    77 ″ ″ ″ 261 270 10 LLLCLIFLLV 1255 A*0206  65 1,71   111 ″ ″ ″ 261 270 10 LLLClIFLLV ″ A*0201  54 1,71    93 ″ ″ ″ 262 270  9 LLCLIFLLV 1256 A*0201   6 1,71    10 ″ ″ ″ 261 271 11 LLLCLIFLLVL 1257 A*0206  85 1,61   136 ″ ″ ″ 261 274 14 LLLCLIFLLVLLDY 1258 A*2902  80 1,83   147 ″ ″ ″ 262 274 13 LLCLIFLLVLLDY 1259 A*2902  90 1,83   165 ″ ″ ″ 262 274 13 LLCLIFLLVLLDY ″ A*0101  75 1,83   138 ″ ″ ″ 264 274 11 CLIFLLVLLDY 1260 A*0101  85 1,83   156 ″ ″ ″ 265 274 10 LIFLLVLLDY 1261 A*0101  55 1,83   101 ″ ″ ″ 265 274 10 LIFLLVLLDY ″ A*0301  35 1,83    64 ″ ″ ″ 266 274  9 IFLLVLLDY 1262 A*2902  70 1,83   128 ″ ″ ″ 267 274  8 FLLVLLDY 1263 B*1502  60 1,83   110 ″ ″ ″ Cumulative Class 10214 I-BCI score: 324 331  8 IPIPSSWA 1264 B*5601  85 0,15    13  32 323 358 324 331  8 IPIPSSWA ″ B*5501  55 0,16     9 ″ ″ ″ 324 332  9 IPIPSSWAF 1265 B*3501  70 1,87   131 ″ ″ ″ 324 332  9 IPIPSSWAF ″ B*3503  55 1,87   103 ″ ″ ″ 324 332  9 IPIPSSWAF ″ B*5301  45 1,87    84 ″ ″ ″ 324 333 10 IPIPSSWAFA 1266 B*5601 100 1,02   102 ″ ″ ″ 324 333 10 IPIPSSWAFA ″ B*5501  85 1,02    87 ″ ″ ″ 326 333  8 IPSSWAFA 1267 B*5601  45 1,02    46 ″ ″ ″ 326 333  8 IPSSWAFA ″ B*5501  40 1,02    41 ″ ″ ″ 323 334 12 CIPIPSSWAFAK 1268 A*0301  80 1,04    83 ″ ″ ″ 323 334 12 CIPIPSSWAFAK ″ A*1101  30 1,04    31 ″ ″ ″ 324 334 11 IPIPSSWAFAK 1269 B*3501  15 1,04    16 ″ ″ ″ 326 334  9 IPSSWAFAK 1270 A*1101  10 1,04    10 ″ ″ ″ 327 334  8 PSSWAFAK 1271 A*0301  45 1,04    47 ″ ″ ″ 324 335 12 IPIPSSWAFAKY 1272 B*3503  85 1,90   161 ″ ″ ″ 324 335 12 IPIPSSWAFAKY ″ B*3501  80 1,90   152 ″ ″ ″ 324 335 12 IPIPSSWAFAKY ″ B*5301  25 1,90    47 ″ ″ ″ 325 335 11 PIPSSWAFAKY 1273 A*2501  30 1,90    57 ″ ″ ″ 326 335 10 IPSSWAFAKY 1274 B*3501  35 1,90    66 ″ ″ ″ 327 335  9 PSSWAFAKY 1275 A*0101  65 1,90   123 ″ ″ ″ 327 335  9 PSSWAFAKY ″ A*3002  45 1,90    85 ″ ″ ″ 328 335  8 SSWAFAKY 1276 A*2501  75 1,90   142 ″ ″ ″ 328 335  8 SSWAFAKY ″ A*3002  75 1,90   142 ″ ″ ″ 328 335  8 SSWAFAKY ″ A*2902  55 1,90   104 ″ ″ ″ 324 336 13 IPIPSSWAFAKYL 1277 B*3503  80 1,06    85 ″ ″ ″ 324 336 13 IPIPSSWAFAKYL ″ B*5101  65 1,06    69 ″ ″ ″ 324 337 14 IPIPSSWAFAKYLW 1278 B*5301  55 1,58    87 ″ ″ ″ 324 337 14 IPIPSSWAFAKYLW ″ B*5101  20 1,58    32 ″ ″ ″ 324 337 14 IPIPSSWAFAKYLW ″ B*5701   5 1,58     8 ″ ″ ″ 326 337 12 IPSSWAFAKYLW 1279 B*5301 100 1,58   158 ″ ″ ″ 326 337 12 IPSSWAFAKYLW ″ B*5802  10 1,58    16 ″ ″ ″ 328 337 10 SSWAFAKYLW 1280 B*5802 100 1,58   158 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5701  95 1,58   150 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4403  45 1,58    71 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5801  35 1,58    55 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4402  15 1,58    24 ″ ″ ″ 330 337  8 WAFAKYLW 1281 B*5801  85 1,58   134 ″ ″ ″ 330 337  8 WAFAKYLW ″ B*5701  65 1,58   103 ″ ″ ″ 330 337  8 WAFAKYLW ″ B*5802  50 1,58    79 326 339 14 IPSSWAFAKYLWEW 1282 B*5301  95 1,83   174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW 1283 B*5701 100 1,83   183 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5801  95 1,83   174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5802  65 1,83   119 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ A*3201  55 1,83   101 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4403  50 1,83    91 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4402  10 1,83    18 ″ ″ ″ 330 339 10 WAFAKYLWEW 1284 B*5802  85 1,83   156 ″ ″ ″ 330 339 10 WAFAKYLWEW ″ B*5201  70 1,83   128 ″ ″ ″ 331 339  9 AFAKYLWEW 1285 B*4402  50 1,83    91 ″ ″ ″ 331 339  9 AFAKYLWEW ″ B*4403  40 1,83    73 ″ ″ ″ 332 339  8 FAKYLWEW 1286 B*4601  40 1,83    73 ″ ″ ″ 332 339  8 FAKYLWEW ″ B*5701  30 1,83    55 ″ ″ ″ 330 342 13 WAFAKYLWEWASV 1287 A*6802  85 1,92   164 ″ ″ ″ 330 342 13 WAFAKYLWEWASV ″ B*1402  20 1,92    38 ″ ″ ″ 332 342 11 FAKYLWEWASV 1288 B*4601  50 1,92    96 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR 1289 A*3303  80 1,07    85 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*6801  50 1,07    53 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*7401  15 1,07    16 ″ ″ ″ 331 343 13 AFAKYLWEWASVR 1290 A*3101  70 1,07    75 ″ ″ ″ 331 343 13 AFAKYLWEWASVR ″ A*3303  35 1,07    37 ″ ″ ″ 332 343 12 FAKYLWEWASVR 1291 A*3303  85 1,07    91 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*6801  60 1,07    64 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*3101  55 1,07    59 ″ ″ ″ 334 343 10 KYLWEWASVR 1292 A*3101 100 1,07   107 ″ ″ ″ 335 343  9 YLWEWASVR 1293 A*7401  85 1,07    91 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*3303  40 1,07    43 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*3101  35 1,07    37 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*0301  20 1,07    21 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF 1294 A*2402  30 1,86    56 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF ″ A*2301   5 1,86     9 ″ ″ ″ 332 344 13 FAKYLWEWASVRF 1295 B*4601  75 1,86   139 ″ ″ ″ 335 344 10 YLWEWASVRF 1296 B*1502  90 1,86   167 ″ ″ ″ 335 344 10 YLWEWASVRF ″ B*1525  45 1,86    84 ″ ″ ″ 337 344  8 WEWASVRF 1297 B*3701  80 1,86   149 ″ ″ ″ 337 344  8 WEWASVRF ″ B*4901  80 1,86   149 ″ ″ ″ 337 344  8 WEWASVRF ″ B*5001  50 1,86    93 ″ ″ ″ 337 344  8 WEWASVRF ″ B*1301  45 1,86    84 ″ ″ ″ 337 344  8 WEWASVRF ″ B*4403   5 1,86     9 ″ ″ ″ 337 345  9 WEWASVRFS 1298 B*4403  65 0,50    33 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*5001  60 0,50    30 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*4002  55 0,50    28 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*4901  15 0,50     8 ″ ″ ″ 333 346 14 AKYLWEWASVRFSW 1299 B*4403  35 1,50    52 ″ ″ ″ 334 346 13 KYLWEWASVRFSW 1300 A*2402  95 1,50   142 ″ ″ ″ 334 346 13 KYLWEWASVRFSW ″ A*2301  75 1,50   112 ″ ″ ″ 335 346 12 YLWEWASVRFSW 1301 A*3201  80 1,50   120 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*1302  75 1,50   112 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*5201  45 1,50    67 ″ ″ ″ 337 346 10 WEWASVRFSW 1302 B*1301 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4402 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4403 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*1302  90 1,50   135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4002  90 1,50   135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4901  75 1,50   112 ″ ″ ″ 339 346  8 WASVRFSW 1303 B*5801  50 1,50    75 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL 1304 A*2402  90 1,37   123 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL ″ A*2301  40 1,37    55 ″ ″ ″ 335 347 13 YLWEWASVRFSWL 1305 A*0201 100 1,37   137 ″ ″ ″ 335 347 13 YLWEWASVRFSWL ″ A*0206  60 1,37    82 ″ ″ ″ 337 347 11 WEWASVRFSWL 1306 B*4001  95 1,37   130 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*3701  90 1,37   123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*5001  90 1,37   123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4002  85 1,37   117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4901  85 1,37   117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1301  80 1,37   110 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4402  55 1,37    75 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1302  10 1,37    14 ″ ″ ″ 339 347  9 WASVRFSWL 1307 B*0801  50 1,37    69 ″ ″ ″ 337 348 12 WEWASVRFSWLS 1308 B*1801  80 0,54    43 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4002  70 0,54    38 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4901  45 0,54    24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*5001  45 0,54    24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4403  20 0,54    11 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*3701   5 0,54     3 ″ ″ ″ 341 348  8 SVRFSWLS 1309 A*3001  40 0,54    22 ″ ″ ″ 337 349 13 WEWASVRFSWLSL 1310 B*1801 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*3701 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4001 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4002 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4901 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*5001 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*1301  90 1,61   145 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4403  75 1,61   120 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4402  70 1,61   112 ″ ″ ″ 339 349 11 WASVRFSWLSL 1311 B*1402  85 1,61   137 ″ ″ ″ 341 349  9 SVRFSWLSL 1312 A*3001  90 1,61   145 ″ ″ ″ 341 349  9 SVRFSWLSL ″ B*0702  80 1,61   129 ″ ″ ″ 342 349  8 VRFSWLSL 1313 B*3901  70 1,61   112 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL 1314 B*3701  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4002  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*5001  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1801  90 1,15   104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4901  90 1,15   104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1301  85 1,15    98 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4001  80 1,15    92 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4403  70 1,15    81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4801  70 1,15    81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4402  60 1,15    69 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1302  50 1,15    58 ″ ″ ″ 342 350  9 VRFSWLSLL 1315 B*3801  65 1,15    75 ″ ″ ″ 342 350  9 VRFSWLSLL ″ B*2702  20 1,15    23 ″ ″ ″ 339 351 13 WASVRFSWLSLLV 1316 B*5101  30 1,47    44 ″ ″ ″ 341 351 11 SVRFSWLSLLV 1317 A*3001  85 1,47   125 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF 1318 B*4601  30 0,19     6 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF ″ B*1525  15 0,19     3 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF 1319 B*1501  80 0,19    15 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1525  60 0,19    11 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1502  25 0,19     5 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ A*3001  20 0,19     4 ″ ″ ″ 342 353 12 VRFSWLSLLVPF 1320 B*2702  65 0,19    12 ″ ″ ″ 342 353 12 VRFSWLSLLVPF ″ B*2705  55 0,19    10 ″ ″ ″ 343 353 11 RFSWLSLLVPF 1321 A*3201  85 0,19    16 ″ ″ ″ 343 353 11 RFSWLSLLVPF ″ A*2402  80 0,19    15 ″ ″ ″ 344 353 10 FSWLSLLVPF 1322 B*4601 100 0,19    19 ″ ″ ″ 344 353 10 FSWLSLLVPF ″ B*1525  55 0,19    10 ″ ″ ″ 346 353  8 WLSLLVPF 1323 B*1502  10 0,19     2 ″ ″ ″ 341 354 14 SVRFSWLSLLVPFV 1324 A*3001  95 1,30   124 ″ ″ ″ 342 354 13 VRFSWLSLLVPFV 1325 B*2705  15 1,30    20 ″ ″ ″ 346 354  9 WLSLLVPFV 1326 A*0201  94 1,30   123 ″ ″ ″ 343 356 14 RFSWLSLLVPFVQW 1327 A*2402  25 1,92    48 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW 1328 B*5801  90 1,92   173 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5701  85 1,92   163 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5802  60 1,92   115 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5201  40 1,92    77 ″ ″ ″ 347 356 10 LSLLVPFVQW 1329 B*5802  80 1,92   154 ″ ″ ″ 344 357 14 FSWLSLLVPFVQWF 1330 B*4601  65 1,38    89 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF 1331 A*2301  45 1,38    62 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF ″ A*2402  35 1,38    48 ″ ″ ″ 347 357 11 LSLLVPFVQWF 1332 B*5802  20 1,38    28 ″ ″ ″ 348 357 10 SLLVPFVQWF 1333 B*1502  50 1,38    69 ″ ″ ″ 349 357  9 LLVPFVQWF 1334 B*1501  45 1,38    62 ″ ″ ″ 349 357  9 LLVPFVQWF ″ B*1525  10 1,38    14 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV 1335 A*0201  80 1,65   132 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV ″ A*0206  25 1,65    41 ″ ″ ″ 349 358 10 LLVPfVQWFV 1336 A*0201  97 1,65   161 ″ ″ ″ 349 358 10 LLVPFVQWFV ″ A*0206  90 1,65   149 ″ ″ ″ 350 358  9 LVPFVQWFV 1337 A*6802 100 1,65   165 ″ ″ ″ 350 358  9 LVPFVQWFV ″ A*0201  43 1,65    71 ″ ″ ″ Cumulative Class 14976 I-BCI score: 327 334  8 PSSWAFAK 1271 A*0301  45 1,04    47  33 327 358 327 335  9 PSSWAFAKY 1275 A*0101  65 1,90   123 ″ ″ ″ 327 335  9 PSSWAFAKY ″ A*3002  45 1,90    85 ″ ″ ″ 328 335  8 SSWAFAKY 1276 A*2501  75 1,90   142 ″ ″ ″ 328 335  8 SSWAFAKY ″ A*3002  75 1,90   142 ″ ″ ″ 328 335  8 SSWAFAKY ″ A*2902  55 1,90   104 ″ ″ ″ 328 337 10 SSWAFAKYLW 1280 B*5802 100 1,58   158 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5701  95 1,58   150 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4403  45 1,58    71 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5801  35 1,58    55 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4402  15 1,58    24 ″ ″ ″ 330 337  8 WAFAKYLW 1281 B*5801  85 1,58   134 ″ ″ ″ 330 337  8 WAFAKYLW ″ B*5701  65 1,58   103 ″ ″ ″ 330 337  8 WAFAKYLW ″ B*5802  50 1,58    79 ″ ″ ″ 328 339 12 SSWAFAKYLWEW 1283 B*5701 100 1,83   183 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5801  95 1,83   174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5802  65 1,83   119 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ A*3201  55 1,83   101 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4403  50 1,83    91 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4402  10 1,83    18 ″ ″ ″ 330 339 10 WAFAKYLWEW 1284 B*5802  85 1,83   156 ″ ″ ″ 330 339 10 WAFAKYLWEW ″ B*5201  70 1,83   128 ″ ″ ″ 331 339  9 AFAKYLWEW 1285 B*4402  50 1,83    91 ″ ″ ″ 331 339  9 AFAKYLWEW ″ B*4403  40 1,83    73 ″ ″ ″ 332 339  8 FAKYLWEW 1286 B*4601  40 1,83    73 ″ ″ ″ 332 339  8 FAKYLWEW ″ B*5701  30 1,83    55 ″ ″ ″ 330 342 13 WAFAKYLWEWASV 1287 A*6802  85 1,92   164 ″ ″ ″ 330 342 13 WAFAKYLWEWASV ″ B*1402  20 1,92    38 ″ ″ ″ 332 342 11 FAKYLWEWASV 1288 B*4601  50 1,92    96 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR 1289 A*3303  80 1,07    85 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*6801  50 1,07    53 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*7401  15 1,07    16 ″ ″ ″ 331 343 13 AFAKYLWEWASVR 1290 A*3101  70 1,07    75 ″ ″ ″ 331 343 13 AFAKYLWEWASVR ″ A*3303  35 1,07    37 ″ ″ ″ 332 343 12 FAKYLWEWASVR 1291 A*3303  85 1,07    91 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*6801  60 1,07    64 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*3101  55 1,07    59 ″ ″ ″ 334 343 10 KYLWEWASVR 1292 A*3101 100 1,07   107 ″ ″ ″ 335 343  9 YLWEWASVR 1293 A*7401  85 1,07    91 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*3303  40 1,07    43 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*3101  35 1,07    37 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*0301  20 1,07    21 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF 1294 A*2402  30 1,86    56 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF ″ A*2301   5 1,86     9 ″ ″ ″ 332 344 13 FAKYLWEWASVRF 1295 B*4601  75 1,86   139 ″ ″ ″ 335 344 10 YLWEWASVRF 1296 B*1502  90 1,86   167 ″ ″ ″ 335 344 10 YLWEWASVRF ″ B*1525  45 1,86    84 ″ ″ ″ 337 344  8 WEWASVRF 1297 B*3701  80 1,86   149 ″ ″ ″ 337 344  8 WEWASVRF ″ B*4901  80 1,86   149 ″ ″ ″ 337 344  8 WEWASVRF ″ B*5001  50 1,86    93 ″ ″ ″ 337 344  8 WEWASVRF ″ B*1301  45 1,86    84 ″ ″ ″ 337 344  8 WEWASVRF ″ B*4403   5 1,86     9 ″ ″ ″ 337 345  9 WEWASVRFS 1298 B*4403  65 0,50    33 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*5001  60 0,50    30 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*4002  55 0,50    28 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*4901  15 0,50     8 ″ ″ ″ 333 346 14 AKYLWEWASVRFSW 1299 B*4403  35 1,50    52 ″ ″ ″ 334 346 13 KYLWEWASVRFSW 1300 A*2402  95 1,50   142 ″ ″ ″ 334 346 13 KYLWEWASVRFSW ″ A*2301  75 1,50   112 ″ ″ ″ 335 346 12 YLWEWASVRFSW 1301 A*3201  80 1,50   120 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*1302  75 1,50   112 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*5201  45 1,50    67 ″ ″ ″ 337 346 10 WEWASVRFSW 1302 B*1301 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4402 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4403 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*1302  90 1,50   135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4002  90 1,50   135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4901  75 1,50   112 ″ ″ ″ 339 346  8 WASVRFSW 1303 B*5801  50 1,50    75 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL 1304 A*2402  90 1,37   123 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL ″ A*2301  40 1,37    55 ″ ″ ″ 335 347 13 YLWEWASVRFSWL 1305 A*0201 100 1,37   137 ″ ″ ″ 335 347 13 YLWEWASVRFSWL ″ A*0206  60 1,37    82 ″ ″ ″ 337 347 11 WEWASVRFSWL 1306 B*4001  95 1,37   130 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*3701  90 1,37   123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*5001  90 1,37   123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4002  85 1,37   117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4901  85 1,37   117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1301  80 1,37   110 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4402  55 1,37    75 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1302  10 1,37    14 ″ ″ ″ 339 347  9 WASVRFSWL 1307 B*0801  50 1,37    69 ″ ″ ″ 337 348 12 WEWASVRFSWLS 1308 B*1801  80 0,54    43 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4002  70 0,54    38 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4901  45 0,54    24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*5001  45 0,54    24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4403  20 0,54    11 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*3701   5 0,54     3 ″ ″ ″ 341 348  8 SVRFSWLS 1309 A*3001  40 0,54    22 ″ ″ ″ 337 349 13 WEWASVRFSWLSL 1310 B*1801 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*3701 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4001 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4002 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4901 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*5001 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*1301  90 1,61   145 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4403  75 1,61   120 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4402  70 1,61   112 ″ ″ ″ 339 349 11 WASVRFSWLSL 1311 B*1402  85 1,61   137 ″ ″ ″ 341 349  9 SVRFSWLSL 1312 A*3001  90 1,61   145 ″ ″ ″ 341 349  9 SVRFSWLSL ″ B*0702  80 1,61   129 ″ ″ ″ 342 349  8 VRFSWLSL 1313 B*3901  70 1,61   112 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL 1314 B*3701  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4002  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*5001  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1801  90 1,15   104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4901  90 1,15   104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1301  85 1,15    98 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4001  80 1,15    92 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4403  70 1,15    81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4801  70 1,15    81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4402  60 1,15    69 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1302  50 1,15    58 ″ ″ ″ 342 350  9 VRFSWLSLL 1315 B*3801  65 1,15    75 ″ ″ ″ 342 350  9 VRFSWLSLL ″ B*2702  20 1,15    23 ″ ″ ″ 339 351 13 WASVRFSWLSLLV 1316 B*5101  30 1,47    44 ″ ″ ″ 341 351 11 SVRFSWLSLLV 1317 A*3001  85 1,47   125 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF 1318 B*4601  30 0,19     6 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF ″ B*1525  15 0,19     3 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF 1319 B*1501  80 0,19    15 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1525  60 0,19    11 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1502  25 0,19     5 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ A*3001  20 0,19     4 ″ ″ ″ 342 353 12 VRFSWLSLLVPF 1320 B*2702  65 0,19    12 ″ ″ ″ 342 353 12 VRFSWLSLLVPF ″ B*2705  55 0,19    10 ″ ″ ″ 343 353 11 RFSWLSLLVPF 1321 A*3201  85 0,19    16 ″ ″ ″ 343 353 11 RFSWLSLLVPF ″ A*2402  80 0,19    15 ″ ″ ″ 344 353 10 FSWLSLLVPF 1322 B*4601 100 0,19    19 ″ ″ ″ 344 353 10 FSWLSLLVPF ″ B*1525  55 0,19    10 ″ ″ ″ 346 353  8 WLSLLVPF 1323 B*1502  10 0,19     2 ″ ″ ″ 341 354 14 SVRFSWLSLLVPFV 1324 A*3001  95 1,30   124 ″ ″ ″ 342 354 13 VRFSWLSLLVPFV 1325 B*2705  15 1,30    20 ″ ″ ″ 346 354  9 WLSLLVPFV 1326 A*0201  94 1,30   123 ″ ″ ″ 343 356 14 RFSWLSLLVPFVQW 1327 A*2402  25 1,92    48 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW 1328 B*5801  90 1,92   173 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5701  85 1,92   163 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5802  60 1,92   115 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5201  40 1,92    77 ″ ″ ″ 347 356 10 LSLLVPFVQW 1329 B*5802  80 1,92   154 ″ ″ ″ 344 357 14 FSWLSLLVPFVQWF 1330 B*4601  65 1,38    89 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF 1331 A*2301  45 1,38    62 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF ″ A*2402  35 1,38    48 ″ ″ ″ 347 357 11 LSLLVPFVQWF 1332 B*5802  20 1,38    28 ″ ″ ″ 348 357 10 SLLVPFVQWF 1333 B*1502  50 1,38    69 ″ ″ ″ 349 357  9 LLVPFVQWF 1334 B*1501  45 1,38    62 ″ ″ ″ 349 357  9 LLVPFVQWF ″ B*1525  10 1,38    14 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV 1335 A*0201  80 1,65   132 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV ″ A*0206  25 1,65    41 ″ ″ ″ 349 358 10 LLVPfVQWFV 1336 A*0201  97 1,65   161 ″ ″ ″ 349 358 10 LLVPFVQWFV ″ A*0206  90 1,65   149 ″ ″ ″ 350 358  9 LVPFVQWFV 1337 A*6802 100 1,65   165 ″ ″ ″ 350 358  9 LVPFVQWFV ″ A*0201  43 1,65    71 ″ ″ ″ Cumulative Class 13107 I-BCI score: 328 335  8 SSWAFAKY 1276 A*2501  75 1,90   142  34 328 358 328 335  8 SSWAFAKY ″ A*3002  75 1,90   142 ″ ″ ″ 328 335  8 SSWAFAKY ″ A*2902  55 1,90   104 ″ ″ ″ 328 337 10 SSWAFAKYLW 1280 B*5802 100 1,58   158 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5701  95 1,58   150 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4403  45 1,58    71 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5801  35 1,58    55 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4402  15 1,58    24 ″ ″ ″ 330 337  8 WAFAKYLW 1281 B*5801  85 1,58   134 ″ ″ ″ 330 337  8 WAFAKYLW ″ B*5701  65 1,58   103 ″ ″ ″ 330 337  8 WAFAKYLW ″ B*5802  50 1,58    79 ″ ″ ″ 328 339 12 SSWAFAKYLWEW 1283 B*5701 100 1,83   183 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5801  95 1,83   174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5802  65 1,83   119 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ A*3201  55 1,83   101 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4403  50 1,83    91 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4402  10 1,83    18 ″ ″ ″ 330 339 10 WAFAKYLWEW 1284 B*5802  85 1,83   156 ″ ″ ″ 330 339 10 WAFAKYLWEW ″ B*5201  70 1,83   128 ″ ″ ″ 331 339  9 AFAKYLWEW 1285 B*4402  50 1,83    91 ″ ″ ″ 331 339  9 AFAKYLWEW ″ B*4403  40 1,83    73 ″ ″ ″ 332 339  8 FAKYLWEW 1286 B*4601  40 1,83    73 ″ ″ ″ 332 339  8 FAKYLWEW ″ B*5701  30 1,83    55 ″ ″ ″ 330 342 13 WAFAKYLWEWASV 1287 A*6802  85 1,92   164 ″ ″ ″ 330 342 13 WAFAKYLWEWASV ″ B*1402  20 1,92    38 ″ ″ ″ 332 342 11 FAKYLWEWASV 1288 B*4601  50 1,92    96 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR 1289 A*3303  80 1,07    85 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*6801  50 1,07    53 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*7401  15 1,07    16 ″ ″ ″ 331 343 13 AFAKYLWEWASVR 1290 A*3101  70 1,07    75 ″ ″ ″ 331 343 13 AFAKYLWEWASVR ″ A*3303  35 1,07    37 ″ ″ ″ 332 343 12 FAKYLWEWASVR 1291 A*3303  85 1,07    91 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*6801  60 1,07    64 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*3101  55 1,07    59 ″ ″ ″ 334 343 10 KYLWEWASVR 1292 A*3101 100 1,07   107 ″ ″ ″ 335 343  9 YLWEWASVR 1293 A*7401  85 1,07    91 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*3303  40 1,07    43 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*3101  35 1,07    37 ″ ″ ″ 335 343  9 YLWEWASVR ″ A*0301  20 1,07    21 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF 1294 A*2402  30 1,86    56 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF ″ A*2301   5 1,86     9 ″ ″ ″ 332 344 13 FAKYLWEWASVRF 1295 B*4601  75 1,86   139 ″ ″ ″ 335 344 10 YLWEWASVRF 1296 B*1502  90 1,86   167 ″ ″ ″ 335 344 10 YLWEWASVRF ″ B*1525  45 1,86    84 ″ ″ ″ 337 344  8 WEWASVRF 1297 B*3701  80 1,86   149 ″ ″ ″ 337 344  8 WEWASVRF ″ B*4901  80 1,86   149 ″ ″ ″ 337 344  8 WEWASVRF ″ B*5001  50 1,86    93 ″ ″ ″ 337 344  8 WEWASVRF ″ B*1301  45 1,86    84 ″ ″ ″ 337 344  8 WEWASVRF ″ B*4403   5 1,86     9 ″ ″ ″ 337 345  9 WEWASVRFS 1298 B*4403  65 0,50    33 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*5001  60 0,50    30 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*4002  55 0,50    28 ″ ″ ″ 337 345  9 WEWASVRFS ″ B*4901  15 0,50     8 ″ ″ ″ 333 346 14 AKYLWEWASVRFSW 1299 B*4403  35 1,50    52 ″ ″ ″ 334 346 13 KYLWEWASVRFSW 1300 A*2402  95 1,50   142 ″ ″ ″ 334 346 13 KYLWEWASVRFSW ″ A*2301  75 1,50   112 ″ ″ ″ 335 346 12 YLWEWASVRFSW 1301 A*3201  80 1,50   120 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*1302  75 1,50   112 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*5201  45 1,50    67 ″ ″ ″ 337 346 10 WEWASVRFSW 1302 B*1301 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4402 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4403 100 1,50   150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*1302  90 1,50   135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4002  90 1,50   135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4901  75 1,50   112 ″ ″ ″ 339 346  8 WASVRFSW 1303 B*5801  50 1,50    75 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL 1304 A*2402  90 1,37   123 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL ″ A*2301  40 1,37    55 ″ ″ ″ 335 347 13 YLWEWASVRFSWL 1305 A*0201 100 1,37   137 ″ ″ ″ 335 347 13 YLWEWASVRFSWL ″ A*0206  60 1,37    82 ″ ″ ″ 337 347 11 WEWASVRFSWL 1306 B*4001  95 1,37   130 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*3701  90 1,37   123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*5001  90 1,37   123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4002  85 1,37   117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4901  85 1,37   117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1301  80 1,37   110 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4402  55 1,37    75 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1302  10 1,37    14 ″ ″ ″ 339 347  9 WASVRFSWL 1307 B*0801  50 1,37    69 ″ ″ ″ 337 348 12 WEWASVRFSWLS 1308 B*1801  80 0,54    43 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4002  70 0,54    38 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4901  45 0,54    24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*5001  45 0,54    24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4403  20 0,54    11 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*3701   5 0,54     3 ″ ″ ″ 341 348  8 SVRFSWLS 1309 A*3001  40 0,54    22 ″ ″ ″ 337 349 13 WEWASVRFSWLSL 1310 B*1801 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*3701 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4001 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4002 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4901 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*5001 100 1,61   161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*1301  90 1,61   145 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4403  75 1,61   120 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4402  70 1,61   112 ″ ″ ″ 339 349 11 WASVRFSWLSL 1311 B*1402  85 1,61   137 ″ ″ ″ 341 349  9 SVRFSWLSL 1312 A*3001  90 1,61   145 ″ ″ ″ 341 349  9 SVRFSWLSL ″ B*0702  80 1,61   129 ″ ″ ″ 342 349  8 VRFSWLSL 1313 B*3901  70 1,61   112 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL 1314 B*3701  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4002  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*5001  95 1,15   109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1801  90 1,15   104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4901  90 1,15   104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1301  85 1,15    98 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4001  80 1,15    92 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4403  70 1,15    81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4801  70 1,15    81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4402  60 1,15    69 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1302  50 1,15    58 ″ ″ ″ 342 350  9 VRFSWLSLL 1315 B*3801  65 1,15    75 ″ ″ ″ 342 350  9 VRFSWLSLL ″ B*2702  20 1,15    23 ″ ″ ″ 339 351 13 WASVRFSWLSLLV 1316 B*5101  30 1,47    44 ″ ″ ″ 341 351 11 SVRFSWLSLLV 1317 A*3001  85 1,47   125 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF 1318 B*4601  30 0,19     6 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF ″ B*1525  15 0,19     3 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF 1319 B*1501  80 0,19    15 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1525  60 0,19    11 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1502  25 0,19     5 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ A*3001  20 0,19     4 ″ ″ ″ 342 353 12 VRFSWLSLLVPF 1320 B*2702  65 0,19    12 ″ ″ ″ 342 353 12 VRFSWLSLLVPF ″ B*2705  55 0,19    10 ″ ″ ″ 343 353 11 RFSWLSLLVPF 1321 A*3201  85 0,19    16 ″ ″ ″ 343 353 11 RFSWLSLLVPF ″ A*2402  80 0,19    15 ″ ″ ″ 344 353 10 FSWLSLLVPF 1322 B*4601 100 0,19    19 ″ ″ ″ 344 353 10 FSWLSLLVPF ″ B*1525  55 0,19    10 ″ ″ ″ 346 353  8 WLSLLVPF 1323 B*1502  10 0,19     2 ″ ″ ″ 341 354 14 SVRFSWLSLLVPFV 1324 A*3001  95 1,30   124 ″ ″ ″ 342 354 13 VRFSWLSLLVPFV 1325 B*2705  15 1,30    20 ″ ″ ″ 346 354  9 WLSLLVPFV 1326 A*0201  94 1,30   123 ″ ″ ″ 343 356 14 RFSWLSLLVPFVQW 1327 A*2402  25 1,92    48 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW 1328 B*5801  90 1,92   173 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5701  85 1,92   163 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5802  60 1,92   115 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5201  40 1,92    77 ″ ″ ″ 347 356 10 LSLLVPFVQW 1329 B*5802  80 1,92   154 ″ ″ ″ 344 357 14 FSWLSLLVPFVQWF 1330 B*4601  65 1,38    89 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF 1331 A*2301  45 1,38    62 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF ″ A*2402  35 1,38    48 ″ ″ ″ 347 357 11 LSLLVPFVQWF 1332 B*5802  20 1,38    28 ″ ″ ″ 348 357 10 SLLVPFVQWF 1333 B*1502  50 1,38    69 ″ ″ ″ 349 357  9 LLVPFVQWF 1334 B*1501  45 1,38    62 ″ ″ ″ 349 357  9 LLVPFVQWF ″ B*1525  10 1,38    14 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV 1335 A*0201  80 1,65   132 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV ″ A*0206  25 1,65    41 ″ ″ ″ 349 358 10 LLVPfVQWFV 1336 A*0201  97 1,65   161 ″ ″ ″ 349 358 10 LLVPFVQWFV ″ A*0206  90 1,65   149 ″ ″ ″ 350 358  9 LVPFVQWFV 1337 A*6802 100 1,65   165 ″ ″ ″ 350 358  9 LVPFVQWFV ″ A*0201  43 1,65    71 ″ ″ ″ Cumulative Class 12851 I-BCI score: 366 373  8 LSAIWMMW 1338 B*5801 100 1,78   178  35 365 400 366 373  8 LSAIWMMW ″ B*5701  60 1,78   107 ″ ″ ″ 366 373  8 LSAIWMMW ″ B*5802  45 1,78    80 ″ ″ ″ 365 374 10 WLSAIWMMWY 1339 A*0101  90 1,38   124 ″ ″ ″ 365 374 10 WLSAIWMMWY ″ A*0301  70 1,38    96 ″ ″ ″ 366 374  9 LSAIWMMWY 1340 A*0101 100 1,38   138 ″ ″ ″ 367 374  8 SAIWMMWY 1341 A*2501  90 1,38   124 ″ ″ ″ 367 374  8 SAIWMMWY ″ A*3002  60 1,38    83 ″ ″ ″ 366 375 10 LSAIWMMWYW 1342 B*5802  95 1,46   139 ″ ″ ″ 366 375 10 LSAIWMMWYW ″ B*5801  75 1,46   110 ″ ″ ″ 367 375  9 SAIWMMWYW 1343 B*5801  80 1,46   117 ″ ″ ″ 367 375  9 SAIWMMWYW ″ B*4403  55 1,46    81 ″ ″ ″ 367 375  9 SAIWMMWYW ″ B*5701  55 1,46    81 ″ ″ ″ 367 375  9 SAIWMMWYW ″ B*4402  45 1,46    66 ″ ″ ″ 367 375  9 SAIWMMWYW ″ B*5301  40 1,46    59 ″ ″ ″ 368 375  8 AIWMMWYW 1344 B*5701  25 1,46    37 ″ ″ ″ 370 379 10 WMMWYWGPSL 1345 B*0801  95 1,46   138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3801  95 1,46   138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3901  95 1,46   138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*4801  80 1,46   117 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3701  65 1,46    95 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1301  40 1,46    58 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1525  20 1,46    29 ″ ″ ″ 371 379  9 MMWYWGPSL 1346 B*4801  85 1,46   124 ″ ″ ″ 371 379  9 MMWYWGPSL ″ B*1525  75 1,46   109 ″ ″ ″ 371 379  9 MMWYWGPSL ″ A*0201  46 1,46    67 ″ ″ ″ 371 379  9 MMWYWGPSL ″ A*3201  45 1,46    66 ″ ″ ″ 371 379  9 MMWYWGPSL ″ B*1501  40 1,46    58 ″ ″ ″ 371 379  9 MMWYWGPSL ″ B*3901  40 1,46    58 ″ ″ ″ 367 380 14 SAIWMMWYWGPSLY 1347 A*2601  95 1,93   183 ″ ″ ″ 367 380 14 SAIWMMWYWGPSLY ″ A*1101  80 1,93   154 ″ ″ ″ 367 380 14 SAIWMMWYWGPSLY ″ B*3501  75 1,93   145 ″ ″ ″ 368 380 13 AIWMMWYWGPSLY 1348 A*3002  85 1,93   164 ″ ″ ″ 370 380 11 WMMWYWGPSLY 1349 B*1502 100 1,93   193 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ A*0101  95 1,93   183 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ B*1501  75 1,93   145 ″ ″ ″ 371 380 10 MMWYWGPSLY 1350 A*0301 100 1,93   193 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*3002  90 1,93   174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ B*1525  90 1,93   174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*7401  80 1,93   154 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*2902  65 1,93   125 ″ ″ ″ 372 380  9 MWYWGPSLY 1351 A*2902 100 1,93   193 ″ ″ ″ 369 382 14 IWMMWYWGPSLYSI 1352 A*2402  85 0,77    65 ″ ″ ″ 369 382 14 IWMMWYWGPSLYSI ″ A*2301  60 0,77    46 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI 1353 A*0206 100 0,77    77 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*0801  85 0,77    65 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*3801  75 0,77    58 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ A*0201  74 0,77    57 ″ ″ ″ 371 382 12 MMWYWGPSLYSI 1354 A*3201 100 0,77    77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*5201 100 0,77    77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1302  95 0,77    73 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*0201  86 0,77    66 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*7401  75 0,77    58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*4801  75 0,77    58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1301  70 0,77    54 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV 1355 A*0206  70 0,79    55 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ A*0201  51 0,79    40 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*0801  45 0,79    35 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3901  10 0,79     8 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3801   5 0,79     4 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV 1356 A*0201  69 0,79    54 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*1302  25 0,79    20 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*4801  25 0,79    20 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF 1357 B*1502  80 0,72    58 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2301  55 0,72    40 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2402  20 0,72    14 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2902  15 0,72    11 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF 1358 A*2301  70 0,72    51 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF ″ A*2402  70 0,72    51 ″ ″ ″ 377 386 10 PSLYSIVSPF 1359 A*3201  35 0,72    25 ″ ″ ″ 378 386  9 SLYSIVSPF 1360 B*1525  95 0,72    69 ″ ″ ″ 378 386  9 SLYSIVSPF ″ A*3201  90 0,72    65 ″ ″ ″ 378 386  9 SLYSIVSPF ″ B*1501  85 0,72    61 ″ ″ ″ 378 386  9 SLYSIVSPF ″ B*4601  20 0,72    14 ″ ″ ″ 378 386  9 SLYSIVSPF ″ A*2601  10 0,72     7 ″ ″ ″ 374 387 14 YWGPSLYSIVSPFI 1361 A*2402  15 1,16    17 ″ ″ ″ 378 387 10 SLYSiVSPFI 1362 A*0201   3 1,16     3 ″ ″ ″ 376 389 14 GPSLYSIVSPFIPL 1363 B*0702  65 0,42    27 ″ ″ ″ 378 389 12 SLYSIVSPFIPL 1364 A*3201  75 0,42    32 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ A*0201  34 0,42    14 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1502  30 0,42    13 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1501   5 0,42     2 ″ ″ ″ 380 389 10 YSIVSPFIPL 1365 B*3901  65 0,42    27 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ A*6802  45 0,42    19 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ B*4001  40 0,42    17 ″ ″ ″ 378 390 13 SLYSIVSPFIPLL 1366 A*0201  17 1,76    30 ″ ″ ″ 379 392 14 LYSIVSPFIPLLPI 1367 A*2402  60 1,07    64 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI 1368 B*4601  45 1,07    48 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI ″ B*5201  30 1,07    32 ″ ″ ″ 381 392 12 SIVSPFIPLLPI 1369 A*6802  25 1,07    27 ″ ″ ″ 382 392 11 IVSPFIPLLPI 1370 A*6802  30 1,07    32 ″ ″ ″ 384 392  9 SPFIPLLPI 1371 B*5501  90 1,07    96 ″ ″ ″ 384 392  9 SPFIPLLPI ″ B*5201  75 1,07    80 ″ ″ ″ 384 392  9 SPFIPLLPI ″ B*5101  70 1,07    75 ″ ″ ″ 384 392  9 SPFIPLLPI ″ B*5601  10 1,07    11 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF 1372 B*4601  85 0,82    69 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*5801  55 0,82    45 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ A*2501  45 0,82    37 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1525  30 0,82    25 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1501  15 0,82    12 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF 1373 B*1525  40 0,82    33 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF ″ A*2601   5 0,82     4 ″ ″ ″ 384 393 10 SPFIPLLPIF 1374 B*3501  65 0,82    53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*3503  65 0,82    53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*5101  45 0,82    37 ″ ″ ″ 385 393  9 PFIPLLPIF 1375 A*2301  15 0,82    12 ″ ″ ″ 386 393  8 FIPLLPIF 1376 A*2501  20 0,82    16 ″ ″ ″ 384 394 11 SPFIPLLPIFF 1377 B*3503 100 1,11   111 ″ ″ ″ 387 394  8 IPLLPIFF 1378 B*3503  70 1,11    78 ″ ″ ″ 386 395 10 FIPLIPIFFC 1379 A*0201   9 0,98     8 ″ ″ ″ 384 396 13 SPFIPLLPIFFCL 1380 B*3503  75 1,93   145 ″ ″ ″ 387 396 10 IPLLPIFFCL 1381 B*5101  10 1,93    19 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW 1382 B*3503  60 1,67   100 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW ″ B*5301  15 1,67    25 ″ ″ ″ 387 397 11 IPLLPIFFCLW 1383 B*5101  55 1,67    92 ″ ″ ″ 387 398 12 IPLLPIFFCLWV 1384 B*5101 100 1,51   151 ″ ″ ″ 389 398 10 LLPIfFCLWV 1385 A*0201  89 1,51   134 ″ ″ ″ 390 398  9 LPIFFCLWV 1386 B*5101  85 1,51   129 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY 1387 A*2501  50 1,83    92 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*0101  35 1,83    64 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*2601  20 1,83    37 ″ ″ ″ 387 399 13 IPLLPIFFCLWVY 1388 B*3501  60 1,83   110 ″ ″ ″ 388 399 12 PLLPIFFCLWVY 1389 A*2902  25 1,83    46 ″ ″ ″ 388 399 12 PLLPIFFCLWVY ″ A*3002  25 1,83    46 ″ ″ ″ 389 399 11 LLPIFFCLWVY 1390 A*0101  60 1,83   110 ″ ″ ″ 390 399 10 LPIFFCLWVY 1391 B*3501  95 1,83   174 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5101  35 1,83    64 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5301  35 1,83    64 ″ ″ ″ 391 399  9 PIFFCLWVY 1392 A*3002  40 1,83    73 ″ ″ ″ 391 399  9 PIFFCLWVY ″ A*2501  25 1,83    46 ″ ″ ″ 392 399  8 IFFCLWVY 1393 A*3002  35 1,83    64 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI 1394 B*5101  90 1,45   131 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI ″ B*5201  20 1,45    29 ″ ″ ″ 390 400 11 LPIFFCLWVYI 1395 B*3503   5 1,45     7 ″ ″ ″ Cumulative Class  9736 I-BCI score: 371 380 10 MMWYWGPSLY 1350 A*0301 100 1,93   193  36 371 400 371 380 10 MMWYWGPSLY ″ A*3002  90 1,93   174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ B*1525  90 1,93   174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*7401  80 1,93   154 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*2902  65 1,93   125 ″ ″ ″ 372 380  9 MWYWGPSLY 1351 A*2902 100 1,93   193 ″ ″ ″ 371 382 12 MMWYWGPSLYSI 1354 A*3201 100 0,77    77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*5201 100 0,77    77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1302  95 0,77    73 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*0201  86 0,77    66 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*7401  75 0,77    58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*4801  75 0,77    58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1301  70 0,77    54 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV 1355 A*0206  70 0,79    55 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ A*0201  51 0,79    40 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*0801  45 0,79    35 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3901  10 0,79     8 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3801   5 0,79     4 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV 1356 A*0201  69 0,79    54 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*1302  25 0,79    20 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*4801  25 0,79    20 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF 1357 B*1502  80 0,72    58 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2301  55 0,72    40 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2402  20 0,72    14 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2902  15 0,72    11 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF 1358 A*2301  70 0,72    51 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF ″ A*2402  70 0,72    51 ″ ″ ″ 377 386 10 PSLYSIVSPF 1359 A*3201  35 0,72    25 ″ ″ ″ 378 386  9 SLYSIVSPF 1360 B*1525  95 0,72    69 ″ ″ ″ 378 386  9 SLYSIVSPF ″ A*3201  90 0,72    65 ″ ″ ″ 378 386  9 SLYSIVSPF ″ B*1501  85 0,72    61 ″ ″ ″ 378 386  9 SLYSIVSPF ″ B*4601  20 0,72    14 ″ ″ ″ 378 386  9 SLYSIVSPF ″ A*2601  10 0,72     7 ″ ″ ″ 374 387 14 YWGPSLYSIVSPFI 1361 A*2402  15 1,16    17 ″ ″ ″ 378 387 10 SLYSiVSPFI 1362 A*0201   3 1,16     3 ″ ″ ″ 376 389 14 GPSLYSIVSPFIPL 1363 B*0702  65 0,42    27 ″ ″ ″ 378 389 12 SLYSIVSPFIPL 1364 A*3201  75 0,42    32 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ A*0201  34 0,42    14 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1502  30 0,42    13 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1501   5 0,42     2 ″ ″ ″ 380 389 10 YSIVSPFIPL 1365 B*3901  65 0,42    27 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ A*6802  45 0,42    19 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ B*4001  40 0,42    17 ″ ″ ″ 378 390 13 SLYSIVSPFIPLL 1366 A*0201  17 1,76    30 ″ ″ ″ 379 392 14 LYSIVSPFIPLLPI 1367 A*2402  60 1,07    64 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI 1368 B*4601  45 1,07    48 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI ″ B*5201  30 1,07    32 ″ ″ ″ 381 392 12 SIVSPFIPLLPI 1369 A*6802  25 1,07    27 ″ ″ ″ 382 392 11 IVSPFIPLLPI 1370 A*6802  30 1,07    32 ″ ″ ″ 384 392  9 SPFIPLLPI 1371 B*5501  90 1,07    96 ″ ″ ″ 384 392  9 SPFIPLLPI ″ B*5201  75 1,07    80 ″ ″ ″ 384 392  9 SPFIPLLPI ″ B*5101  70 1,07    75 ″ ″ ″ 384 392  9 SPFIPLLPI ″ B*5601  10 1,07    11 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF 1372 B*4601  85 0,82    69 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*5801  55 0,82    45 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ A*2501  45 0,82    37 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1525  30 0,82    25 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1501  15 0,82    12 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF 1373 B*1525  40 0,82    33 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF ″ A*2601   5 0,82     4 ″ ″ ″ 384 393 10 SPFIPLLPIF 1374 B*3501  65 0,82    53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*3503  65 0,82    53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*5101  45 0,82    37 ″ ″ ″ 385 393  9 PFIPLLPIF 1375 A*2301  15 0,82    12 ″ ″ ″ 386 393  8 FIPLLPIF 1376 A*2501  20 0,82    16 ″ ″ ″ 384 394 11 SPFIPLLPIFF 1377 B*3503 100 1,11   111 ″ ″ ″ 387 394  8 IPLLPIFF 1378 B*3503  70 1,11    78 ″ ″ ″ 386 395 10 FIPLIPIFFC 1379 A*0201   9 0,98     8 ″ ″ ″ 384 396 13 SPFIPLLPIFFCL 1380 B*3503  75 1,93   145 ″ ″ ″ 387 396 10 IPLLPIFFCL 1381 B*5101  10 1,93    19 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW 1382 B*3503  60 1,67   100 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW ″ B*5301  15 1,67    25 ″ ″ ″ 387 397 11 IPLLPIFFCLW 1383 B*5101  55 1,67    92 ″ ″ ″ 387 398 12 IPLLPIFFCLWV 1384 B*5101 100 1,51   151 ″ ″ ″ 389 398 10 LLPIfFCLWV 1385 A*0201  89 1,51   134 ″ ″ ″ 390 398  9 LPIFFCLWV 1386 B*5101  85 1,51   129 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY 1387 A*2501  50 1,83    92 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*0101  35 1,83    64 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*2601  20 1,83    37 ″ ″ ″ 387 399 13 IPLLPIFFCLWVY 1388 B*3501  60 1,83   110 ″ ″ ″ 388 399 12 PLLPIFFCLWVY 1389 A*2902  25 1,83    46 ″ ″ ″ 388 399 12 PLLPIFFCLWVY ″ A*3002  25 1,83    46 ″ ″ ″ 389 399 11 LLPIFFCLWVY 1390 A*0101  60 1,83   110 ″ ″ ″ 390 399 10 LPIFFCLWVY 1391 B*3501  95 1,83   174 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5101  35 1,83    64 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5301  35 1,83    64 ″ ″ ″ 391 399  9 PIFFCLWVY 1392 A*3002  40 1,83    73 ″ ″ ″ 391 399  9 PIFFCLWVY ″ A*2501  25 1,83    46 ″ ″ ″ 392 399  8 IFFCLWVY 1393 A*3002  35 1,83    64 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI 1394 B*5101  90 1,45   131 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI ″ B*5201  20 1,45    29 ″ ″ ″ 390 400 11 LPIFFCLWVYI 1395 B*3503   5 1,45     7 ″ ″ ″ Cumulative Class  5389 I-BCI score: 370 379 10 WMMWYWGPSL 1345 B*0801  95 1,46   138  37 370 400 370 379 10 WMMWYWGPSL ″ B*3801  95 1,46   138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3901  95 1,46   138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*4801  80 1,46   117 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3701  65 1,46    95 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1301  40 1,46    58 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1525  20 1,46    29 ″ ″ ″ 370 380 11 WMMWYWGPSLY 1349 B*1502 100 1,93   193 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ A*0101  95 1,93   183 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ B*1501  75 1,93   145 ″ ″ ″ 371 380 10 MMWYWGPSLY 1350 A*0301 100 1,93   193 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*3002  90 1,93   174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ B*1525  90 1,93   174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*7401  80 1,93   154 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*2902  65 1,93   125 ″ ″ ″ 372 380  9 MWYWGPSLY 1351 A*2902 100 1,93   193 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI 1353 A*0206 100 0,77    77 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*0801  85 0,77    65 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*3801  75 0,77    58 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ A*0201  74 0,77    57 ″ ″ ″ 371 382 12 MMWYWGPSLYSI 1354 A*3201 100 0,77    77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*5201 100 0,77    77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1302  95 0,77    73 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*0201  86 0,77    66 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*7401  75 0,77    58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*4801  75 0,77    58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1301  70 0,77    54 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV 1355 A*0206  70 0,79    55 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ A*0201  51 0,79    40 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*0801  45 0,79    35 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3901  10 0,79     8 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3801   5 0,79     4 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV 1356 A*0201  69 0,79    54 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*1302  25 0,79    20 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*4801  25 0,79    20 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF 1357 B*1502  80 0,72    58 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2301  55 0,72    40 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2402  20 0,72    14 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2902  15 0,72    11 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF 1358 A*2301  70 0,72    51 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF ″ A*2402  70 0,72    51 ″ ″ ″ 377 386 10 PSLYSIVSPF 1359 A*3201  35 0,72    25 ″ ″ ″ 378 386  9 SLYSIVSPF 1360 B*1525  95 0,72    69 ″ ″ ″ 378 386  9 SLYSIVSPF ″ A*3201  90 0,72    65 ″ ″ ″ 378 386  9 SLYSIVSPF ″ B*1501  85 0,72    61 ″ ″ ″ 378 386  9 SLYSIVSPF ″ B*4601  20 0,72    14 ″ ″ ″ 378 386  9 SLYSIVSPF ″ A*2601  10 0,72     7 ″ ″ ″ 374 387 14 YWGPSLYSIVSPFI 1361 A*2402  15 1,16    17 ″ ″ ″ 378 387 10 SLYSiVSPFI 1362 A*0201   3 1,16     3 ″ ″ ″ 376 389 14 GPSLYSIVSPFIPL 1363 B*0702  65 0,42    27 ″ ″ ″ 378 389 12 SLYSIVSPFIPL 1364 A*3201  75 0,42    32 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ A*0201  34 0,42    14 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1502  30 0,42    13 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1501   5 0,42     2 ″ ″ ″ 380 389 10 YSIVSPFIPL 1365 B*3901  65 0,42    27 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ A*6802  45 0,42    19 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ B*4001  40 0,42    17 ″ ″ ″ 378 390 13 SLYSIVSPFIPLL 1366 A*0201  17 1,76    30 ″ ″ ″ 379 392 14 LYSIVSPFIPLLPI 1367 A*2402  60 1,07    64 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI 1368 B*4601  45 1,07    48 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI ″ B*5201  30 1,07    32 ″ ″ ″ 381 392 12 SIVSPFIPLLPI 1369 A*6802  25 1,07    27 ″ ″ ″ 382 392 11 IVSPFIPLLPI 1370 A*6802  30 1,07    32 ″ ″ ″ 384 392  9 SPFIPLLPI 1371 B*5501  90 1,07    96 ″ ″ ″ 384 392  9 sPFIPLLPI ″ B*5201  75 1,07    80 ″ ″ ″ 384 392  9 sPFIPLLPI ″ B*5101  70 1,07    75 ″ ″ ″ 384 392  9 SPFIPLLPI ″ B*5601  10 1,07    11 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF 1372 B*4601  85 0,82    69 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*5801  55 0,82    45 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ A*2501  45 0,82    37 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1525  30 0,82    25 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1501  15 0,82    12 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF 1373 B*1525  40 0,82    33 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF ″ A*2601   5 0,82     4 ″ ″ ″ 384 393 10 SPFIPLLPIF 1374 B*3501  65 0,82    53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*3503  65 0,82    53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*5101  45 0,82    37 ″ ″ ″ 385 393  9 PFIPLLPIF 1375 A*2301  15 0,82    12 ″ ″ ″ 386 393  8 FIPLLPIF 1376 A*2501  20 0,82    16 ″ ″ ″ 384 394 11 SPFIPLLPIFF 1377 B*3503 100 1,11   111 ″ ″ ″ 387 394  8 IPLLPIFF 1378 B*3503  70 1,11    78 ″ ″ ″ 386 395 10 FIPLIPIFFC 1379 A*0201   9 0,98     8 ″ ″ ″ 384 396 13 SPFIPLLPIFFCL 1380 B*3503  75 1,93   145 ″ ″ ″ 387 396 10 IPLLPIFFCL 1381 B*5101  10 1,93    19 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW 1382 B*3503  60 1,67   100 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW ″ B*5301  15 1,67    25 ″ ″ ″ 387 397 11 IPLLPIFFCLW 1383 B*5101  55 1,67    92 ″ ″ ″ 387 398 12 IPLLPIFFCLWV 1384 B*5101 100 1,51   151 ″ ″ ″ 389 398 10 LLPIfFCLWV 1385 A*0201  89 1,51   134 ″ ″ ″ 390 398  9 LPIFFCLWV 1386 B*5101  85 1,51   129 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY 1387 A*2501  50 1,83    92 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*0101  35 1,83    64 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*2601  20 1,83    37 ″ ″ ″ 387 399 13 IPLLPIFFCLWVY 1388 B*3501  60 1,83   110 ″ ″ ″ 388 399 12 PLLPIFFCLWVY 1389 A*2902  25 1,83    46 ″ ″ ″ 388 399 12 PLLPIFFCLWVY ″ A*3002  25 1,83    46 ″ ″ ″ 389 399 11 LLPIFFCLWVY 1390 A*0101  60 1,83   110 ″ ″ ″ 390 399 10 LPIFFCLWVY 1391 B*3501  95 1,83   174 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5101  35 1,83    64 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5301  35 1,83    64 ″ ″ ″ 391 399  9 PIFFCLWVY 1392 A*3002  40 1,83    73 ″ ″ ″ 391 399  9 PIFFCLWVY ″ A*2501  25 1,83    46 ″ ″ ″ 392 399  8 IFFCLWVY 1393 A*3002  35 1,83    64 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI 1394 B*5101  90 1,45   131 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI ″ B*5201  20 1,45    29 ″ ″ ″ 390 400 11 LPIFFCLWVYI 1395 B*3503   5 1,45     7 ″ ″ ″ Cumulative Class  6880 I-BCI score: “Start” and “End” are relative to the amino acid sequence of HBV large surface protein as depicted in SEQ ID NO: 1141 ^(A)Peptide amino acid sequence. Each HLA class I binding peptide of HBV large surface protein is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods (Examples section). ^(C)C-score. See Material and Methods (Examples section). ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 7b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV large surface protein. HLA class II binding peptides in SLP derived from HBV Surface antigen  SEQ HLA- Peptide of invention (SLP) ID DRB1 ClassII- SLP Start End Sequence^(A) NO: molecule B score^(B) SLP# Start SLP End 181 195 GFLGPLLVLQAGFFL 1396 *1501 85 30 175 210 181 195 GFLGPLLVLQAGFFL ″ *0101 60 ″ ″ ″ 181 195 GFLGPLLVLQAGFFL ″ *1301 53 ″ ″ ″ 181 195 GFLGPLLVLQAGFFL ″ *0102 8 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL 1397 *0101 93 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *1501 83 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *1301 50 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *0102 35 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *0104 28 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *0106 20 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT 1398 *0101 90 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *1501 80 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *1301 48 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *0104 30 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *0102 13 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *0106 8 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR 1399 *1501 78 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0101 58 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *1301 45 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0104 33 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0102 10 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0106 3 ″ ″ ″ 185 199 PLLVLQAGFFLLTRI 1400 *1501 75 ″ ″ ″ 185 199 PLLVLQAGFFLLTRI ″ *1301 43 ″ ″ ″ 185 199 PLLVLQAGFFLLTRI ″ *0101 13 ″ ″ ″ 186 200 LLVLQAGFFLLTRIL 1401 *1301 40 ″ ″ ″ 186 200 LLVLQAGFFLLTRIL ″ *1501 25 ″ ″ ″ 187 201 LVLQAGFFLLTRILT 1402 *1101 83 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *0101 40 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *0701 40 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *1301 38 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *1501 15 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *0301 10 ″ ″ ″ 188 202 VLQAGFFLLTRILTI 1403 *0401 93 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0701 80 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *1101 80 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0101 70 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0104 20 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0102 15 ″ ″ ″ 189 203 LQAGFFLLTRILTIP 1404 *0401 90 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0701 78 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *1101 78 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0101 50 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0104 35 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0102 33 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ 1405 *0401 100 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0701 75 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *1101 75 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0101 68 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0102 63 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0104 58 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *1501 20 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0105 8 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0107 8 ″ ″ ″ 191 205 AGFFLLTRILTIPQS 1406 *0401 98 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0701 73 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *1101 73 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0102 70 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0104 65 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0101 55 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0106 23 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0105 10 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0107 10 ″ ″ ″ 192 206 GFFLLTRILTIPQSL 1407 *0401 95 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *1301 85 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0102 83 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0104 80 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0701 70 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *1101 70 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0106 50 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0105 28 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0107 28 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0101 18 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *1501 10 ″ ″ ″ 193 207 FFLLTRILTIPQSLD 1408 *0401 88 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0102 75 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *1301 75 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0701 68 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *1101 68 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0104 63 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0106 48 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0101 18 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0105 18 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0107 18 ″ ″ ″ 194 208 FLLTRILTIPQSLDS 1409 *0401 85 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *1301 65 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0102 58 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *1101 53 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0106 43 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0104 40 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0701 3 ″ ″ ″ 195 209 LLTRILTIPQSLDSW ″ *1301 70 ″ ″ ″ 195 209 LLTRILTIPQSLDSW ″ *0102 45 ″ ″ ″ 195 209 LLTRILTIPQSLDSW ″ *0106 35 ″ ″ ″ 195 209 LLTRILTIPQSLDSW 1410 *0401 15 ″ ″ ″ 196 210 LTRILTIPQSLDSWW 1411 *1301 45 ″ ″ ″ Cumulative Class 11-B score: 4798 240 254 PPICPGYRWMCLRRF 1412 *1301 83 31 239 274 240 254 PPICPGYRWMCLRRF ″ *1101 70 ″ ″ ″ 241 255 PICPGYRWMCLRRFI 1413 *1301 80 ″ ″ ″ 241 255 PICPGYRWMCLRRFI ″ *1101 80 ″ ″ ″ 241 255 PICPGYRWMCLRRFI ″ *1501 60 ″ ″ ″ 241 255 PICPGYRWMCLRRFI ″ *0701 35 ″ ″ ″ 242 256 ICPGYRWMCLRRFII 1414 *1301 78 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *1501 95 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *1101 90 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0701 85 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0104 70 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0102 68 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0101 50 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0105 50 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0107 50 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0301 35 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF 1415 *1301 75 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *1101 5 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *1501 100 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0701 95 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0104 85 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0102 80 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0101 58 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0105 58 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0107 58 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0301 40 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL 1416 *1301 73 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *1101 95 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *1501 90 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0701 80 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0104 75 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0102 73 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0101 45 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0105 45 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0107 45 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0301 15 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF 1417 *1301 100 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0701 48 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *1501 20 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *1101 85 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0102 60 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0104 60 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0101 30 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0105 30 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0107 30 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI 1418 *1301 98 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI ″ *0701 50 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI ″ *1501 23 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI ″ *1101 75 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL 1419 *1301 95 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL ″ *0701 30 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL ″ *1501 10 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL ″ *1101 45 ″ ″ ″ 248 262 WMCLRRFIIFLFILL 1420 *1301 93 ″ ″ ″ 248 262 WMCLRRFIIFLFILL ″ *1501 73 ″ ″ ″ 248 262 WMCLRRFIIFLFILL ″ *0701 60 ″ ″ ″ 248 262 WMCLRRFIIFLFILL ″ *0301 28 ″ ″ ″ 249 263 MCLRRFIIFLFILLL 1421 *1501 95 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *1301 90 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0301 80 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0701 58 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0101 53 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *1101 50 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0401 3 ″ ″ ″ 250 264 CLRRFIIFLFILLLC 1422 *1301 88 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *0301 78 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *1501 68 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *0701 55 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *0101 48 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *1101 48 ″ ″ ″ 251 265 LRRFIIFLFILLLCL 1423 *1501 100 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *1301 85 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *0101 83 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *0301 83 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *1101 58 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *0701 53 ″ ″ ″ 252 266 RRFIIFLFILLLCLI 1424 *1501 98 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *0101 80 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *1101 55 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *0301 40 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *0701 38 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *1301 35 ″ ″ ″ 253 267 RFIIFLFILLLCLIF 1425 *1101 100 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0101 78 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *1501 60 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0301 38 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0701 35 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *1301 33 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0401 8 ″ ″ ″ 254 268 FIIFLFILLLCLIFL 1426 *1101 98 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *1501 88 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *0101 65 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *0301 35 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *1301 30 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *0401 13 ″ ″ ″ 255 269 IIFLFILLLCLIFLL 1427 *1101 95 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *1501 93 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *0301 70 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *0101 35 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *0401 35 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *1301 28 ″ ″ ″ 256 270 IFLFILLLCLIFLLV 1428 *1101 93 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *0301 68 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *1501 53 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *0101 30 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *1301 25 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *0401 10 ″ ″ ″ 257 271 FLFILLLCLIFLLVL 1429 *1101 90 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *0301 65 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *1501 58 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *0101 28 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *1301 23 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *0401 18 ″ ″ ″ 258 272 LFILLLCLIFLLVLL 1430 *1101 88 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *0301 63 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *1501 50 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *0101 25 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *1301 20 ″ ″ ″ 259 273 FILLLCLIFLLVLLD 1431 *1101 85 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *0301 55 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *1501 30 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *0101 23 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *1301 18 ″ ″ ″ 260 274 ILLLCLIFLLVLLDY 1432 *1101 45 ″ ″ ″ 260 274 ILLLCLIFLLVLLDY ″ *1301 15 ″ ″ ″ 260 274 ILLLCLIFLLVLLDY ″ *1501 13 ″ ″ ″ Cumulative Class 11-B score: 7238 330 344 WAFAKYLWEWASVRF 1433 *1501 5 32 323 358 331 345 AFAKYLWEWASVRFS 1434 *0401 65 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *0301 30 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1501 15 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1101 5 ″ ″ ″ 332 346 FAKYLWEWASVRFSW 1435 *0401 80 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0301 55 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1501 50 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1101 40 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0104 25 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0101 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0105 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0107 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0701 15 ″ ″ ″ 333 347 AKYLWEWASVRFSWL 1436 *0701 28 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0401 60 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0301 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *1101 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0101 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0105 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0107 3 ″ ″ ″ 334 348 KYLWEWASVRFSWLS 1437 *0701 25 ″ ″ ″ 334 348 KYLWEWASVRFSWLS ″ *0401 5 ″ ″ ″ 336 350 LWEWASVRFSWLSLL 1438 *0301 33 ″ ″ ″ 337 351 WEWASVRFSWLSLLV 1439 *0301 73 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1501 45 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1301 25 ″ ″ ″ 338 352 EWASVRFSWLSLLVP 1440 *0301 30 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1501 40 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1301 35 ″ ″ ″ 339 353 WASVRFSWLSLLVPF 1441 *0301 58 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1501 55 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1301 50 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0104 38 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0102 5 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV 1442 *0301 75 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0401 33 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1101 18 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0104 53 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1501 30 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0102 28 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1301 20 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0106 10 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ 1443 *0401 30 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *1101 15 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0104 50 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0102 23 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0106 5 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW 1444 *0401 28 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0101 15 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *1101 13 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0104 15 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF 1445 *0401 25 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *0101 20 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *1101 10 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV 1446 *1501 90 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1301 70 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *0401 23 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1101 8 ″ ″ ″ Cumulative Class 11-B score: 1815 ″ 330 344 WAFAKYLWEWASVRF 1433 *1501 5 33 327 358 331 345 AFAKYLWEWASVRFS 1434 *0401 65 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *0301 30 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1501 15 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1101 5 ″ ″ ″ 332 346 FAKYLWEWASVRFSW 1435 *0401 80 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0301 55 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1501 50 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1101 40 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0104 25 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0101 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0105 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0107 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0701 15 ″ ″ ″ 333 347 AKYLWEWASVRFSWL 1436 *0701 28 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0401 60 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0301 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *1101 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0101 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0105 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0107 3 ″ ″ ″ 334 348 KYLWEWASVRFSWLS 1437 *0701 25 ″ ″ ″ 334 348 KYLWEWASVRFSWLS ″ *0401 5 ″ ″ ″ 336 350 LWEWASVRFSWLSLL 1438 *0301 33 ″ ″ ″ 337 351 WEWASVRFSWLSLLV 1439 *0301 73 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1501 45 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1301 25 ″ ″ ″ 338 352 EWASVRFSWLSLLVP 1440 *0301 30 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1501 40 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1301 35 ″ ″ ″ 339 353 WASVRFSWLSLLVPF 1441 *0301 58 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1501 55 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1301 50 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0104 38 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0102 5 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV 1442 *0301 75 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0401 33 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1101 18 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0104 53 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1501 30 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0102 28 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1301 20 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0106 10 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ 1443 *0401 30 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *1101 15 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0104 50 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0102 23 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0106 5 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW 1444 *0401 28 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0101 15 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *1101 13 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0104 15 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF 1445 *0401 25 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *0101 20 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *1101 10 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV 1446 *1501 90 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1301 70 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *0401 23 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1101 8 ″ ″ ″ Cumulative Class 11-B score: 1815 330 344 WAFAKYLWEWASVRF 1433 *1501 5 34 328 358 331 345 AFAKYLWEWASVRFS 1434 *0401 65 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *0301 30 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1501 15 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1101 5 ″ ″ ″ 332 346 FAKYLWEWASVRFSW 1435 *0401 80 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0301 55 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1501 50 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1101 40 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0104 25 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0101 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0105 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0107 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0701 15 ″ ″ ″ 333 347 AKYLWEWASVRFSWL 1436 *0701 28 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0401 60 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0301 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *1101 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0101 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0105 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0107 3 ″ ″ ″ 334 348 KYLWEWASVRFSWLS 1437 *0701 25 ″ ″ ″ 334 348 KYLWEWASVRFSWLS ″ *0401 5 ″ ″ ″ 336 350 LWEWASVRFSWLSLL 1438 *0301 33 ″ ″ ″ 337 351 WEWASVRFSWLSLLV 1439 *0301 73 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1501 45 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1301 25 ″ ″ ″ 338 352 EWASVRFSWLSLLVP 1440 *0301 30 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1501 40 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1301 35 ″ ″ ″ 339 353 WASVRFSWLSLLVPF 1441 *0301 58 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1501 55 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1301 50 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0104 38 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0102 5 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV 1442 *0301 75 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0401 33 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1101 18 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0104 53 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1501 30 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0102 28 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1301 20 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0106 10 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ 1443 *0401 30 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *1101 15 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0104 50 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0102 23 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0106 5 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW 1444 *0401 28 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0101 15 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *1101 13 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0104 15 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF 1445 *0401 25 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *0101 20 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *1101 10 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV 1446 *1501 90 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1301 70 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *0401 23 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1101 8 ″ ″ ″ Cumulative Class 11-B score: 1815 365 379 WLSAIWMMWYWGPSL 1447 *1501 35 35 365 400 366 380 LSAIWMMWYWGPSLY 1448 *1501 48 ″ ″ ″ 367 381 SAIWMMWYWGPSLYS 1449 *1501 40 ″ ″ ″ 368 382 AIWMMWYWGPSLYSI 1450 *1501 45 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV 1451 *1501 38 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV ″ *0101 20 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV ″ *0105 20 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV ″ *0107 20 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS 1452 *1501 28 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0101 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0105 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0107 33 ″ ″ ″ 371 385 MMWYWGPSLYSIVSP 1453 *1501 8 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI 1454 *0701 90 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0401 40 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0106 45 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0101 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0105 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0107 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0102 18 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP 1455 *0701 65 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0101 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0105 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0107 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0401 55 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0106 53 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0102 48 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0104 43 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *1501 25 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL 1456 *0701 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0401 20 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1501 18 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0104 88 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0102 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0101 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0105 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0106 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0107 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0103 15 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1101 15 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL 1457 *0701 83 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0401 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1501 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0101 33 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0104 100 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0102 98 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0105 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0107 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0106 90 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0103 50 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1101 35 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1301 15 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP 1458 *0701 63 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1501 33 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0101 10 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0401 5 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0104 93 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0102 90 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0106 85 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0105 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0107 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0103 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1101 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1301 10 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI 1459 *0701 43 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0104 83 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0102 78 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0106 73 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0101 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0105 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0107 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *1501 35 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0401 20 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0103 5 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF 1460 *0701 33 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0106 63 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0102 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0104 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0101 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0105 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0107 53 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF 1461 *1101 35 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0101 8 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0104 23 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0106 18 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0105 5 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0107 5 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC 1462 *1101 33 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC ″ *0101 5 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL 1463 *1101 30 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0101 3 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0104 18 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0105 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0107 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0102 3 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW 1464 *1101 28 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0101 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0105 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0107 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0104 10 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV 1465 *1101 25 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV ″ *1501 5 ″ ″ ″ 386 400 FIPLLPIFFCLWVYI 1466 *1101 23 ″ ″ ″ Cumulative Class 11-B score: 4425 371 385 MMWYWGPSLYSIVSP 1453 *1501 8 36 371 400 373 387 WYWGPSLYSIVSPFI 1454 *0701 90 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0401 40 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0106 45 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0101 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0105 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0107 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0102 18 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP 1455 *0701 65 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0101 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0105 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0107 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0401 55 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0106 53 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0102 48 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0104 43 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *1501 25 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL 1456 *0701 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0401 20 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1501 18 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0104 88 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0102 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0101 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0105 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0106 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0107 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0103 15 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1101 15 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL 1457 *0701 83 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0401 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1501 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0101 33 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0104 100 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0102 98 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0105 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0107 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0106 90 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0103 50 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1101 35 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1301 15 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP 1458 *0701 63 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1501 33 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0101 10 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0401 5 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0104 93 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0102 90 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0106 85 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0105 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0107 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0103 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1101 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1301 10 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI 1459 *0701 43 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0104 83 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0102 78 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0106 73 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0101 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0105 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0107 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *1501 35 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0401 20 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0103 5 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF 1460 *0701 33 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0106 63 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0102 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0104 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0101 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0105 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0107 53 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF 1461 *1101 35 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0101 8 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0104 23 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0106 18 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0105 5 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0107 5 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC 1462 *1101 33 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC ″ *0101 5 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL 1463 *1101 30 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0101 3 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0104 18 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0105 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0107 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0102 3 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW 1464 *1101 28 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0101 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0105 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0107 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0104 10 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV 1465 *1101 25 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV ″ *1501 5 ″ ″ ″ 386 400 FIPLLPIFFCLWVYI 1466 *1101 23 ″ ″ ″ Cumulative Class 11-B score: 4035 370 384 WMMWYWGPSLYSIVS 1452 *1501 28 37 370 400 370 384 WMMWYWGPSLYSIVS ″ *0101 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0105 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0107 33 ″ ″ ″ 371 385 MMWYWGPSLYSIVSP 1453 *1501 8 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI 1454 *0701 90 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0401 40 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0106 45 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0101 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0105 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0107 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0102 18 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP 1455 *0701 65 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0101 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0105 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0107 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0401 55 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0106 53 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0102 48 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0104 43 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *1501 25 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL 1456 *0701 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0401 20 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1501 18 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0104 88 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0102 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0101 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0105 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0106 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0107 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0103 15 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1101 15 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL 1457 *0701 83 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0401 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1501 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0101 33 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0104 100 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0102 98 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0105 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0107 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0106 90 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0103 50 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1101 35 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1301 15 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP 1458 *0701 63 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1501 33 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0101 10 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0401 5 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0104 93 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0102 90 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0106 85 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0105 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0107 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0103 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1101 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1301 10 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI 1459 *0701 43 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0104 83 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0102 78 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0106 73 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0101 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0105 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0107 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *1501 35 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0401 20 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0103 5 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF 1460 *0701 33 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0106 63 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0102 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0104 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0101 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0105 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0107 53 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF 1461 *1101 35 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0101 8 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0104 23 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0106 18 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0105 5 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0107 5 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC 1462 *1101 33 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC ″ *0101 5 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL 1463 *1101 30 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0101 3 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0104 18 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0105 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0107 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0102 3 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW 1464 *1101 28 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0101 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0105 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0107 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0104 10 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV 1465 *1101 25 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV ″ *1501 5 ″ ″ ″ 386 400 FIPLLPIFFCLWVYI 1466 *1101 23 ″ ″ ″ Cumulative Class 11-B score: 4160 ″Start″ and ″End″ are relative to the amino acid sequence of human HBV large surface protein as depicted in SEQ ID NO: 1141 ^(A)Peptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV large surface protein is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)B-score. See Material and Methods (Examples section). ^(C)Cumulative B-score. See Material and Methods (Examples section).

REFERENCE LIST

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1. A method for the prevention and/or treatment of an HBV-related disease comprising administering to a subject an effective amount of a peptide of at least 30 and at most 40 amino acids in length and comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-79, 1142-1145 and 1468-1471.
 2. The method according to claim 1, wherein the peptide is in an immunogenic pharmaceutical composition.
 3. The method according to claim 2, wherein the composition further comprises an immune-stimulating amount of at least one pharmaceutically acceptable adjuvant.
 4. The method according to claim 3, wherein the pharmaceutically acceptable adjuvant is selected from the group consisting of a human toll-like receptor ligand and/or agonist, Montanide ISA-51, Montanide ISA-720, dsRNA, cyclic dinucleotides (CDNs), Muramyl dipeptide (MDP), a tetanus toxin derived peptide, Interferon alpha (INFα), and combinations thereof.
 5. The method according to claim 1, wherein the administration comprises administration of an additional peptide and/or of a polynucleotide encoding such a peptide.
 6. The method according to claim 1, wherein the peptide comprises an amino acid sequence of any of the proteins selected from the group consisting of HBV polymerase, HBV core protein, HBV X-protein and HBV large surface protein.
 7. The method according to claim 1, wherein the peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-53, 55, 57, 60, 63, 64, 66, 68, 71, 72, 74-78, 1142, 1145, 1468-1471.
 8. The method according to claim 1, wherein the peptide further comprises a covalently linked functional group, an oligonucleotide conjugate, a sugar chain or glycan, or combinations thereof.
 9. The method according to claim 4, wherein the human toll-like receptor ligand and/or agonist is selected from the group consisting of Gram positive bacterial glycolipid, LPS, LPA, LTA, fimbriae, an outer membrane protein, a heat shock protein, Mycobacterial lipoarabinomannans, dsRNA, poly(I:C), Gram negative bacterial glycolipid, a viral coat protein, a viral envelope protein, taxol and/or derivative thereof, hyaluronan containing oligosaccharides and fibronectins, bacterial flagellae, flagellin, Mycobacterial lipoproteins, group B Streptococcus heat labile soluble factor, a Staphylococcus modulin, imidazoquinolines, imiquimod and/or derivative thereof, resiquimod and/or derivative thereof, unmethylated CpG DNA, chromatin-IgG complexes, IC31, IMSAVAC, pam3cys and/or derivative thereof, poly-ICLC, and CpG oligodeoxynucleotides (CpG-ODNs).
 10. The method according to claim 2, wherein the composition further comprises PSA, 2-aminoisobutyric acid (Abu), a DC pulse cassette, or combinations thereof.
 11. The method according to claim 1, wherein the HBV-related disease is selected from the group consisting of acute HBV infection, chronic HBV infection, conditions where the hepatitis virus is found in the blood or body fluids containing blood of a subject, liver cirrhosis, liver cancer, and presence of the virus in the body of a subject.
 12. The method according to claim 1, wherein the method is for treatment of an HBV-related disease.
 13. A method for the prevention and/or treatment of an HBV-related disease comprising administering to a subject an effective amount of a polynucleotide encoding a peptide of at least 30 and at most 40 amino acids in length, the peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-79, 1142-1145 and 1468-1471.
 14. The method according to claim 13, wherein the polynucleotide is in an immunogenic pharmaceutical composition.
 15. The method according to claim 14, wherein the composition further comprises an immune-stimulating amount of at least one pharmaceutically acceptable adjuvant.
 16. The method according to claim 15, wherein the pharmaceutically acceptable adjuvant is selected from the group consisting of a human toll-like receptor ligand and/or agonist, Montanide ISA-51, Montanide ISA-720, dsRNA, cyclic dinucleotides (CDNs), Muramyl dipeptide (MDP), a tetanus toxin derived peptide, Interferon alpha (INFα), and combinations thereof.
 17. The method according to claim 13, wherein the administration comprises administration of an additional polynucleotide and/or of a peptide as defined in claim
 18. 18. The method according to claim 13, wherein the peptide comprises an amino acid sequence of any of the proteins selected from the group consisting of HBV polymerase, HBV core protein, HBV X-protein and HBV large surface protein.
 19. The method according to claim 13, wherein the peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-53, 55, 57, 60, 63, 64, 66, 68, 71, 72, 74-78, 1142, 1145, 1468-1471.
 20. The method according to claim 13, wherein the polynucleotide further comprises a covalently linked functional group, an oligonucleotide conjugate, a sugar chain or glycan, or combinations thereof.
 21. The method according to claim 16, wherein the human toll-like receptor ligand and/or agonist is selected from the group consisting of Gram positive bacterial glycolipid, LPS, LPA, LTA, fimbriae, an outer membrane protein, a heat shock protein, Mycobacterial lipoarabinomannans, dsRNA, poly(I:C), Gram negative bacterial glycolipid, a viral coat protein, a viral envelope protein, taxol and/or derivative thereof, hyaluronan containing oligosaccharides and fibronectins, bacterial flagellae, flagellin, Mycobacterial lipoproteins, group B Streptococcus heat labile soluble factor, a Staphylococcus modulin, imidazoquinolines, imiquimod and/or derivative thereof, resiquimod and/or derivative thereof, unmethylated CpG DNA, chromatin-IgG complexes, IC31, IMSAVAC, pam3cys and/or derivative thereof, poly-ICLC, and CpG oligodeoxynucleotides (CpG-ODNs).
 22. The method according to claim 14, wherein the composition further comprises PSA, 2-aminoisobutyric acid (Abu), a DC pulse cassette, or combinations thereof.
 23. The method according to claim 13, wherein the HBV-related disease is selected from the group consisting of acute HBV infection, chronic HBV infection, conditions where the hepatitis virus is found in the blood or body fluids containing blood of a subject, liver cirrhosis, liver cancer, and presence of the virus in the body of a subject. 